---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '21913'
abstract:
- lang: eng
  text: 'The HIRA histone chaperone complex is comprised of four protein subunits:
    HIRA, UBN1, CABIN1, and transiently associated ASF1a. All four subunits have been
    demonstrated to play a role in the deposition of the histone variant H3.3 onto
    areas of actively transcribed euchromatin in cells. The mechanism by which these
    subunits function together to drive histone deposition has remained poorly understood.
    Here we present biochemical and biophysical data supporting a model whereby ASF1a
    delivers histone H3.3/H4 dimers to the HIRA complex, H3.3/H4 tetramerization drives
    the association of two HIRA/UBN1 complexes, and the affinity of the histones for
    DNA drives release of ASF1a and subsequent histone deposition. These findings
    have implications for understanding how other histone chaperone complexes may
    mediate histone deposition.'
acknowledgement: We would like to acknowledge Elliot Dean and Christina Freeman for
  technical assistance with recombinant protein expression in insect cells and members
  of the Marmorstein laboratory for many discussions related to this work. Schematic
  Figures were created with BioRender.com.
article_number: '107604'
article_processing_charge: Yes
article_type: original
author:
- first_name: Austin
  full_name: Vogt, Austin
  last_name: Vogt
- first_name: Mary
  full_name: Szurgot, Mary
  last_name: Szurgot
- first_name: Lauren
  full_name: Gardner, Lauren
  id: f9dedd98-6d15-11f0-88a5-a7b4143fdec5
  last_name: Gardner
  orcid: 0009-0000-5733-1546
- first_name: David C.
  full_name: Schultz, David C.
  last_name: Schultz
- first_name: Ronen
  full_name: Marmorstein, Ronen
  last_name: Marmorstein
citation:
  ama: Vogt A, Szurgot M, Gardner L, Schultz DC, Marmorstein R. HIRA complex deposition
    of histone H3.3 is driven by histone tetramerization and histone-DNA binding.
    <i>Journal of Biological Chemistry</i>. 2024;300(9). doi:<a href="https://doi.org/10.1016/j.jbc.2024.107604">10.1016/j.jbc.2024.107604</a>
  apa: Vogt, A., Szurgot, M., Gardner, L., Schultz, D. C., &#38; Marmorstein, R. (2024).
    HIRA complex deposition of histone H3.3 is driven by histone tetramerization and
    histone-DNA binding. <i>Journal of Biological Chemistry</i>. Elsevier. <a href="https://doi.org/10.1016/j.jbc.2024.107604">https://doi.org/10.1016/j.jbc.2024.107604</a>
  chicago: Vogt, Austin, Mary Szurgot, Lauren Gardner, David C. Schultz, and Ronen
    Marmorstein. “HIRA Complex Deposition of Histone H3.3 Is Driven by Histone Tetramerization
    and Histone-DNA Binding.” <i>Journal of Biological Chemistry</i>. Elsevier, 2024.
    <a href="https://doi.org/10.1016/j.jbc.2024.107604">https://doi.org/10.1016/j.jbc.2024.107604</a>.
  ieee: A. Vogt, M. Szurgot, L. Gardner, D. C. Schultz, and R. Marmorstein, “HIRA
    complex deposition of histone H3.3 is driven by histone tetramerization and histone-DNA
    binding,” <i>Journal of Biological Chemistry</i>, vol. 300, no. 9. Elsevier, 2024.
  ista: Vogt A, Szurgot M, Gardner L, Schultz DC, Marmorstein R. 2024. HIRA complex
    deposition of histone H3.3 is driven by histone tetramerization and histone-DNA
    binding. Journal of Biological Chemistry. 300(9), 107604.
  mla: Vogt, Austin, et al. “HIRA Complex Deposition of Histone H3.3 Is Driven by
    Histone Tetramerization and Histone-DNA Binding.” <i>Journal of Biological Chemistry</i>,
    vol. 300, no. 9, 107604, Elsevier, 2024, doi:<a href="https://doi.org/10.1016/j.jbc.2024.107604">10.1016/j.jbc.2024.107604</a>.
  short: A. Vogt, M. Szurgot, L. Gardner, D.C. Schultz, R. Marmorstein, Journal of
    Biological Chemistry 300 (2024).
date_created: 2026-05-24T08:25:45Z
date_published: 2024-09-01T00:00:00Z
date_updated: 2026-06-02T14:52:50Z
day: '01'
ddc:
- '572'
doi: 10.1016/j.jbc.2024.107604
extern: '1'
external_id:
  pmid:
  - '39059488'
fulldoi: https://doi.org/10.1016/j.jbc.2024.107604
has_accepted_license: '1'
intvolume: '       300'
issue: '9'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/j.jbc.2024.107604
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: HIRA complex deposition of histone H3.3 is driven by histone tetramerization
  and histone-DNA binding
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 300
year: '2024'
...
---
_id: '12082'
abstract:
- lang: eng
  text: Proximity-dependent protein labeling provides a powerful in vivo strategy
    to characterize the interactomes of specific proteins. We previously optimized
    a proximity labeling protocol for Caenorhabditis elegans using the highly active
    biotin ligase TurboID. A significant constraint on the sensitivity of TurboID
    is the presence of abundant endogenously biotinylated proteins that take up bandwidth
    in the mass spectrometer, notably carboxylases that use biotin as a cofactor.
    In C. elegans, these comprise POD-2/acetyl-CoA carboxylase alpha, PCCA-1/propionyl-CoA
    carboxylase alpha, PYC-1/pyruvate carboxylase, and MCCC-1/methylcrotonyl-CoA carboxylase
    alpha. Here, we developed ways to remove these carboxylases prior to streptavidin
    purification and mass spectrometry by engineering their corresponding genes to
    add a C-terminal His10 tag. This allows us to deplete them from C. elegans lysates
    using immobilized metal affinity chromatography. To demonstrate the method's efficacy,
    we use it to expand the interactome map of the presynaptic active zone protein
    ELKS-1. We identify many known active zone proteins, including UNC-10/RIM, SYD-2/liprin-alpha,
    SAD-1/BRSK1, CLA-1/CLArinet, C16E9.2/Sentryn, as well as previously uncharacterized
    potentially synaptic proteins such as the ortholog of human angiomotin, F59C12.3
    and the uncharacterized protein R148.3. Our approach provides a quick and inexpensive
    solution to a common contaminant problem in biotin-dependent proximity labeling.
    The approach may be applicable to other model organisms and will enable deeper
    and more complete analysis of interactors for proteins of interest.
acknowledged_ssus:
- _id: Bio
acknowledgement: "We thank de Bono laboratory members for helpful comments on the
  article and the Mass Spec Facilities at IST Austria and Max Perutz Labs for invaluable
  discussions and comments on how to optimize mass spec analyses of worm samples.
  We are grateful to Ekaterina Lashmanova for designing the degron knock-in constructs
  and preparing the injection mixes for CRISPR/Cas9-mediated genome editing. All LC–MS/MS
  analyses were performed on instruments of the Vienna BioCenter Core Facilities instrument
  pool.\r\nThis work was supported by a Wellcome Investigator Award (grant no.: 209504/Z/17/Z
  ) to M.d.B. and an ISTplus Fellowship to M.A. (Marie Sklodowska-Curie agreement
  no.: 754411)."
article_number: '102343'
article_processing_charge: No
article_type: original
author:
- first_name: Murat
  full_name: Artan, Murat
  id: C407B586-6052-11E9-B3AE-7006E6697425
  last_name: Artan
  orcid: 0000-0001-8945-6992
- first_name: Markus
  full_name: Hartl, Markus
  last_name: Hartl
- first_name: Weiqiang
  full_name: Chen, Weiqiang
  last_name: Chen
- first_name: Mario
  full_name: De Bono, Mario
  id: 4E3FF80E-F248-11E8-B48F-1D18A9856A87
  last_name: De Bono
  orcid: 0000-0001-8347-0443
citation:
  ama: Artan M, Hartl M, Chen W, de Bono M. Depletion of endogenously biotinylated
    carboxylases enhances the sensitivity of TurboID-mediated proximity labeling in
    Caenorhabditis elegans. <i>Journal of Biological Chemistry</i>. 2022;298(9). doi:<a
    href="https://doi.org/10.1016/j.jbc.2022.102343">10.1016/j.jbc.2022.102343</a>
  apa: Artan, M., Hartl, M., Chen, W., &#38; de Bono, M. (2022). Depletion of endogenously
    biotinylated carboxylases enhances the sensitivity of TurboID-mediated proximity
    labeling in Caenorhabditis elegans. <i>Journal of Biological Chemistry</i>. Elsevier.
    <a href="https://doi.org/10.1016/j.jbc.2022.102343">https://doi.org/10.1016/j.jbc.2022.102343</a>
  chicago: Artan, Murat, Markus Hartl, Weiqiang Chen, and Mario de Bono. “Depletion
    of Endogenously Biotinylated Carboxylases Enhances the Sensitivity of TurboID-Mediated
    Proximity Labeling in Caenorhabditis Elegans.” <i>Journal of Biological Chemistry</i>.
    Elsevier, 2022. <a href="https://doi.org/10.1016/j.jbc.2022.102343">https://doi.org/10.1016/j.jbc.2022.102343</a>.
  ieee: M. Artan, M. Hartl, W. Chen, and M. de Bono, “Depletion of endogenously biotinylated
    carboxylases enhances the sensitivity of TurboID-mediated proximity labeling in
    Caenorhabditis elegans,” <i>Journal of Biological Chemistry</i>, vol. 298, no.
    9. Elsevier, 2022.
  ista: Artan M, Hartl M, Chen W, de Bono M. 2022. Depletion of endogenously biotinylated
    carboxylases enhances the sensitivity of TurboID-mediated proximity labeling in
    Caenorhabditis elegans. Journal of Biological Chemistry. 298(9), 102343.
  mla: Artan, Murat, et al. “Depletion of Endogenously Biotinylated Carboxylases Enhances
    the Sensitivity of TurboID-Mediated Proximity Labeling in Caenorhabditis Elegans.”
    <i>Journal of Biological Chemistry</i>, vol. 298, no. 9, 102343, Elsevier, 2022,
    doi:<a href="https://doi.org/10.1016/j.jbc.2022.102343">10.1016/j.jbc.2022.102343</a>.
  short: M. Artan, M. Hartl, W. Chen, M. de Bono, Journal of Biological Chemistry
    298 (2022).
corr_author: '1'
date_created: 2022-09-11T22:01:55Z
date_published: 2022-09-01T00:00:00Z
date_updated: 2025-04-14T07:44:00Z
day: '01'
ddc:
- '570'
department:
- _id: MaDe
doi: 10.1016/j.jbc.2022.102343
ec_funded: 1
external_id:
  isi:
  - '000884241800011'
  pmid:
  - '35933017'
file:
- access_level: open_access
  checksum: e726c7b9315230e6710e0b1f1d1677e9
  content_type: application/pdf
  creator: dernst
  date_created: 2022-09-12T08:14:50Z
  date_updated: 2022-09-12T08:14:50Z
  file_id: '12092'
  file_name: 2022_JBC_Artan.pdf
  file_size: 2101656
  relation: main_file
  success: 1
file_date_updated: 2022-09-12T08:14:50Z
fulldoi: https://doi.org/10.1016/j.jbc.2022.102343
has_accepted_license: '1'
intvolume: '       298'
isi: 1
issue: '9'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 23870BE8-32DE-11EA-91FC-C7463DDC885E
  grant_number: 209504/A/17/Z
  name: Molecular mechanisms of neural circuit function
- _id: 260C2330-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '754411'
  name: ISTplus - Postdoctoral Fellowships
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Depletion of endogenously biotinylated carboxylases enhances the sensitivity
  of TurboID-mediated proximity labeling in Caenorhabditis elegans
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 298
year: '2022'
...
---
_id: '10117'
abstract:
- lang: eng
  text: Proximity labeling provides a powerful in vivo tool to characterize the proteome
    of subcellular structures and the interactome of specific proteins. The nematode
    Caenorhabditis elegans is one of the most intensely studied organisms in biology,
    offering many advantages for biochemistry. Using the highly active biotin ligase
    TurboID, we optimize here a proximity labeling protocol for C. elegans. An advantage
    of TurboID is that biotin's high affinity for streptavidin means biotin-labeled
    proteins can be affinity-purified under harsh denaturing conditions. By combining
    extensive sonication with aggressive denaturation using SDS and urea, we achieved
    near-complete solubilization of worm proteins. We then used this protocol to characterize
    the proteomes of the worm gut, muscle, skin, and nervous system. Neurons are among
    the smallest C. elegans cells. To probe the method's sensitivity, we expressed
    TurboID exclusively in the two AFD neurons and showed that the protocol could
    identify known and previously unknown proteins expressed selectively in AFD. The
    active zones of synapses are composed of a protein matrix that is difficult to
    solubilize and purify. To test if our protocol could solubilize active zone proteins,
    we knocked TurboID into the endogenous elks-1 gene, which encodes a presynaptic
    active zone protein. We identified many known ELKS-1-interacting active zone proteins,
    as well as previously uncharacterized synaptic proteins. Versatile vectors and
    the inherent advantages of using C. elegans, including fast growth and the ability
    to rapidly make and functionally test knock-ins, make proximity labeling a valuable
    addition to the armory of this model organism.
acknowledgement: We thank de Bono lab members for helpful comments on the manuscript,
  IST Austria and University of Vienna Mass Spec Facilities for invaluable discussions
  and comments for the optimization of mass spec analyses of worm samples. The biotin
  auxotropic E. coli strain MG1655bioB:kan was gift from John Cronan (University of
  Illinois) and was kindly sent to us by Jessica Feldman and Ariana Sanchez (Stanford
  University). dg398 pEntryslot2_mNeongreen::3XFLAG::stop and dg397 pEntryslot3_mNeongreen::3XFLAG::stop::unc-54
  3′UTR entry vector were kindly shared by Dr Dominique Glauser (University of Fribourg).
  Codon-optimized mScarlet vector was a generous gift from Dr Manuel Zimmer (University
  of Vienna).
article_number: '101094'
article_processing_charge: Yes
article_type: original
author:
- first_name: Murat
  full_name: Artan, Murat
  id: C407B586-6052-11E9-B3AE-7006E6697425
  last_name: Artan
  orcid: 0000-0001-8945-6992
- first_name: Stephen
  full_name: Barratt, Stephen
  id: 57740d2b-2a88-11ec-97cf-d9e6d1b39677
  last_name: Barratt
- first_name: Sean M.
  full_name: Flynn, Sean M.
  last_name: Flynn
- first_name: Farida
  full_name: Begum, Farida
  last_name: Begum
- first_name: Mark
  full_name: Skehel, Mark
  last_name: Skehel
- first_name: Armel
  full_name: Nicolas, Armel
  id: 2A103192-F248-11E8-B48F-1D18A9856A87
  last_name: Nicolas
- first_name: Mario
  full_name: De Bono, Mario
  id: 4E3FF80E-F248-11E8-B48F-1D18A9856A87
  last_name: De Bono
  orcid: 0000-0001-8347-0443
citation:
  ama: Artan M, Barratt S, Flynn SM, et al. Interactome analysis of Caenorhabditis
    elegans synapses by TurboID-based proximity labeling. <i>Journal of Biological
    Chemistry</i>. 2021;297(3). doi:<a href="https://doi.org/10.1016/J.JBC.2021.101094">10.1016/J.JBC.2021.101094</a>
  apa: Artan, M., Barratt, S., Flynn, S. M., Begum, F., Skehel, M., Nicolas, A., &#38;
    de Bono, M. (2021). Interactome analysis of Caenorhabditis elegans synapses by
    TurboID-based proximity labeling. <i>Journal of Biological Chemistry</i>. Elsevier.
    <a href="https://doi.org/10.1016/J.JBC.2021.101094">https://doi.org/10.1016/J.JBC.2021.101094</a>
  chicago: Artan, Murat, Stephen Barratt, Sean M. Flynn, Farida Begum, Mark Skehel,
    Armel Nicolas, and Mario de Bono. “Interactome Analysis of Caenorhabditis Elegans
    Synapses by TurboID-Based Proximity Labeling.” <i>Journal of Biological Chemistry</i>.
    Elsevier, 2021. <a href="https://doi.org/10.1016/J.JBC.2021.101094">https://doi.org/10.1016/J.JBC.2021.101094</a>.
  ieee: M. Artan <i>et al.</i>, “Interactome analysis of Caenorhabditis elegans synapses
    by TurboID-based proximity labeling,” <i>Journal of Biological Chemistry</i>,
    vol. 297, no. 3. Elsevier, 2021.
  ista: Artan M, Barratt S, Flynn SM, Begum F, Skehel M, Nicolas A, de Bono M. 2021.
    Interactome analysis of Caenorhabditis elegans synapses by TurboID-based proximity
    labeling. Journal of Biological Chemistry. 297(3), 101094.
  mla: Artan, Murat, et al. “Interactome Analysis of Caenorhabditis Elegans Synapses
    by TurboID-Based Proximity Labeling.” <i>Journal of Biological Chemistry</i>,
    vol. 297, no. 3, 101094, Elsevier, 2021, doi:<a href="https://doi.org/10.1016/J.JBC.2021.101094">10.1016/J.JBC.2021.101094</a>.
  short: M. Artan, S. Barratt, S.M. Flynn, F. Begum, M. Skehel, A. Nicolas, M. de
    Bono, Journal of Biological Chemistry 297 (2021).
date_created: 2021-10-10T22:01:23Z
date_published: 2021-09-01T00:00:00Z
date_updated: 2025-04-14T07:43:46Z
day: '01'
ddc:
- '612'
department:
- _id: MaDe
- _id: LifeSc
doi: 10.1016/J.JBC.2021.101094
ec_funded: 1
external_id:
  isi:
  - '000706409200006'
file:
- access_level: open_access
  checksum: 19e39d36c5b9387c6dc0e89c9ae856ab
  content_type: application/pdf
  creator: cchlebak
  date_created: 2021-10-11T12:20:58Z
  date_updated: 2021-10-11T12:20:58Z
  file_id: '10121'
  file_name: 2021_JBC_Artan.pdf
  file_size: 1680010
  relation: main_file
  success: 1
file_date_updated: 2021-10-11T12:20:58Z
fulldoi: https://doi.org/10.1016/J.JBC.2021.101094
has_accepted_license: '1'
intvolume: '       297'
isi: 1
issue: '3'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
project:
- _id: 260C2330-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '754411'
  name: ISTplus - Postdoctoral Fellowships
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Interactome analysis of Caenorhabditis elegans synapses by TurboID-based proximity
  labeling
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 297
year: '2021'
...
---
_id: '7880'
abstract:
- lang: eng
  text: 'Following its evoked release, dopamine (DA) signaling is rapidly terminated
    by presynaptic reuptake, mediated by the cocaine-sensitive DA transporter (DAT).
    DAT surface availability is dynamically regulated by endocytic trafficking, and
    direct protein kinase C (PKC) activation acutely diminishes DAT surface expression
    by accelerating DAT internalization. Previous cell line studies demonstrated that
    PKC-stimulated DAT endocytosis requires both Ack1 inactivation, which releases
    a DAT-specific endocytic brake, and the neuronal GTPase, Rit2, which binds DAT.
    However, it is unknown whether Rit2 is required for PKC-stimulated DAT endocytosis
    in DAergic terminals or whether there are region- and/or sex-dependent differences
    in PKC-stimulated DAT trafficking. Moreover, the mechanisms by which Rit2 controls
    PKC-stimulated DAT endocytosis are unknown. Here, we directly examined these important
    questions. Ex vivo studies revealed that PKC activation acutely decreased DAT
    surface expression selectively in ventral, but not dorsal, striatum. AAV-mediated,
    conditional Rit2 knockdown in DAergic neurons impacted baseline DAT surface:intracellular
    distribution in DAergic terminals from female ventral, but not dorsal, striatum.
    Further, Rit2 was required for PKC-stimulated DAT internalization in both male
    and female ventral striatum. FRET and surface pulldown studies in cell lines revealed
    that PKC activation drives DAT-Rit2 surface dissociation and that the DAT N terminus
    is required for both PKC-mediated DAT-Rit2 dissociation and DAT internalization.
    Finally, we found that Rit2 and Ack1 independently converge on DAT to facilitate
    PKC-stimulated DAT endocytosis. Together, our data provide greater insight into
    mechanisms that mediate PKC-regulated DAT internalization and reveal unexpected
    region-specific differences in PKC-stimulated DAT trafficking in bona fide DAergic
    terminals. '
article_processing_charge: No
article_type: original
author:
- first_name: Rita R.
  full_name: Fagan, Rita R.
  last_name: Fagan
- first_name: Patrick J.
  full_name: Kearney, Patrick J.
  last_name: Kearney
- first_name: Carolyn G.
  full_name: Sweeney, Carolyn G.
  last_name: Sweeney
- first_name: Dino
  full_name: Luethi, Dino
  last_name: Luethi
- first_name: Florianne E
  full_name: Schoot Uiterkamp, Florianne E
  id: 3526230C-F248-11E8-B48F-1D18A9856A87
  last_name: Schoot Uiterkamp
- first_name: Klaus
  full_name: Schicker, Klaus
  last_name: Schicker
- first_name: Brian S.
  full_name: Alejandro, Brian S.
  last_name: Alejandro
- first_name: Lauren C.
  full_name: O'Connor, Lauren C.
  last_name: O'Connor
- first_name: Harald H.
  full_name: Sitte, Harald H.
  last_name: Sitte
- first_name: Haley E.
  full_name: Melikian, Haley E.
  last_name: Melikian
citation:
  ama: 'Fagan RR, Kearney PJ, Sweeney CG, et al. Dopamine transporter trafficking
    and Rit2 GTPase: Mechanism of action and in vivo impact. <i>Journal of Biological
    Chemistry</i>. 2020;295(16):5229-5244. doi:<a href="https://doi.org/10.1074/jbc.RA120.012628">10.1074/jbc.RA120.012628</a>'
  apa: 'Fagan, R. R., Kearney, P. J., Sweeney, C. G., Luethi, D., Schoot Uiterkamp,
    F. E., Schicker, K., … Melikian, H. E. (2020). Dopamine transporter trafficking
    and Rit2 GTPase: Mechanism of action and in vivo impact. <i>Journal of Biological
    Chemistry</i>. ASBMB Publications. <a href="https://doi.org/10.1074/jbc.RA120.012628">https://doi.org/10.1074/jbc.RA120.012628</a>'
  chicago: 'Fagan, Rita R., Patrick J. Kearney, Carolyn G. Sweeney, Dino Luethi, Florianne
    E Schoot Uiterkamp, Klaus Schicker, Brian S. Alejandro, Lauren C. O’Connor, Harald
    H. Sitte, and Haley E. Melikian. “Dopamine Transporter Trafficking and Rit2 GTPase:
    Mechanism of Action and in Vivo Impact.” <i>Journal of Biological Chemistry</i>.
    ASBMB Publications, 2020. <a href="https://doi.org/10.1074/jbc.RA120.012628">https://doi.org/10.1074/jbc.RA120.012628</a>.'
  ieee: 'R. R. Fagan <i>et al.</i>, “Dopamine transporter trafficking and Rit2 GTPase:
    Mechanism of action and in vivo impact,” <i>Journal of Biological Chemistry</i>,
    vol. 295, no. 16. ASBMB Publications, pp. 5229–5244, 2020.'
  ista: 'Fagan RR, Kearney PJ, Sweeney CG, Luethi D, Schoot Uiterkamp FE, Schicker
    K, Alejandro BS, O’Connor LC, Sitte HH, Melikian HE. 2020. Dopamine transporter
    trafficking and Rit2 GTPase: Mechanism of action and in vivo impact. Journal of
    Biological Chemistry. 295(16), 5229–5244.'
  mla: 'Fagan, Rita R., et al. “Dopamine Transporter Trafficking and Rit2 GTPase:
    Mechanism of Action and in Vivo Impact.” <i>Journal of Biological Chemistry</i>,
    vol. 295, no. 16, ASBMB Publications, 2020, pp. 5229–44, doi:<a href="https://doi.org/10.1074/jbc.RA120.012628">10.1074/jbc.RA120.012628</a>.'
  short: R.R. Fagan, P.J. Kearney, C.G. Sweeney, D. Luethi, F.E. Schoot Uiterkamp,
    K. Schicker, B.S. Alejandro, L.C. O’Connor, H.H. Sitte, H.E. Melikian, Journal
    of Biological Chemistry 295 (2020) 5229–5244.
date_created: 2020-05-24T22:00:59Z
date_published: 2020-04-17T00:00:00Z
date_updated: 2025-07-10T11:54:48Z
day: '17'
department:
- _id: SaSi
doi: 10.1074/jbc.RA120.012628
external_id:
  isi:
  - '000530288000006'
  pmid:
  - '32132171'
fulldoi: https://doi.org/10.1074/jbc.RA120.012628
intvolume: '       295'
isi: 1
issue: '16'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://escholarship.umassmed.edu/oapubs/4187
month: '04'
oa: 1
oa_version: Submitted Version
page: 5229-5244
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: ASBMB Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Dopamine transporter trafficking and Rit2 GTPase: Mechanism of action and
  in vivo impact'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 295
year: '2020'
...
---
_id: '8440'
abstract:
- lang: eng
  text: Mycobacterium tuberculosis can remain dormant in the host, an ability that
    explains the failure of many current tuberculosis treatments. Recently, the natural
    products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill
    Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of
    the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein
    substrates, such as proteins containing phosphorylated arginine residues, to the
    ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit
    ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using
    NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding
    to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these
    dynamics are caused by conformational changes and do not result from unfolding
    or oligomerization of this domain. Cyclomarin binding to this domain specifically
    blocked these N-terminal dynamics. On the basis of these results, we propose a
    mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics,
    which modulates the chaperone enzymatic activity leading eventually to cell death.
article_processing_charge: No
article_type: original
author:
- first_name: Katharina
  full_name: Weinhäupl, Katharina
  last_name: Weinhäupl
- first_name: Martha
  full_name: Brennich, Martha
  last_name: Brennich
- first_name: Uli
  full_name: Kazmaier, Uli
  last_name: Kazmaier
- first_name: Joel
  full_name: Lelievre, Joel
  last_name: Lelievre
- first_name: Lluis
  full_name: Ballell, Lluis
  last_name: Ballell
- first_name: Alfred
  full_name: Goldberg, Alfred
  last_name: Goldberg
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Hugo
  full_name: Fraga, Hugo
  last_name: Fraga
citation:
  ama: Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks
    arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1
    from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. 2018;293(22):8379-8393.
    doi:<a href="https://doi.org/10.1074/jbc.ra118.002251">10.1074/jbc.ra118.002251</a>
  apa: Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg,
    A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced
    millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
    <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38;
    Molecular Biology. <a href="https://doi.org/10.1074/jbc.ra118.002251">https://doi.org/10.1074/jbc.ra118.002251</a>
  chicago: Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis
    Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin
    Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain
    of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry &#38; Molecular Biology, 2018. <a href="https://doi.org/10.1074/jbc.ra118.002251">https://doi.org/10.1074/jbc.ra118.002251</a>.
  ieee: K. Weinhäupl <i>et al.</i>, “The antibiotic cyclomarin blocks arginine-phosphate–induced
    millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,”
    <i>Journal of Biological Chemistry</i>, vol. 293, no. 22. American Society for
    Biochemistry &#38; Molecular Biology, pp. 8379–8393, 2018.
  ista: Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda
    P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced
    millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
    Journal of Biological Chemistry. 293(22), 8379–8393.
  mla: Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced
    Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.”
    <i>Journal of Biological Chemistry</i>, vol. 293, no. 22, American Society for
    Biochemistry &#38; Molecular Biology, 2018, pp. 8379–93, doi:<a href="https://doi.org/10.1074/jbc.ra118.002251">10.1074/jbc.ra118.002251</a>.
  short: K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg,
    P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.
date_created: 2020-09-18T10:05:18Z
date_published: 2018-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '01'
doi: 10.1074/jbc.ra118.002251
extern: '1'
fulldoi: https://doi.org/10.1074/jbc.ra118.002251
intvolume: '       293'
issue: '22'
keyword:
- Cell Biology
- Biochemistry
- Molecular Biology
language:
- iso: eng
month: '06'
oa_version: None
page: 8379-8393
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
  - 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics
  in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 293
year: '2018'
...
---
_id: '668'
abstract:
- lang: eng
  text: Macrophage filopodia, finger-like membrane protrusions, were first implicated
    in phagocytosis more than 100 years ago, but little is still known about the involvement
    of these actin-dependent structures in particle clearance. Using spinning disk
    confocal microscopy to image filopodial dynamics in mouse resident Lifeact-EGFP
    macrophages, we show that filopodia, or filopodia-like structures, support pathogen
    clearance by multiple means. Filopodia supported the phagocytic uptake of bacterial
    (Escherichia coli) particles by (i) capturing along the filopodial shaft and surfing
    toward the cell body, the most common mode of capture; (ii) capturing via the
    tip followed by retraction; (iii) combinations of surfing and retraction; or (iv)
    sweeping actions. In addition, filopodia supported the uptake of zymosan (Saccharomyces
    cerevisiae) particles by (i) providing fixation, (ii) capturing at the tip and
    filopodia-guided actin anterograde flow with phagocytic cup formation, and (iii)
    the rapid growth of new protrusions. To explore the role of filopodia-inducing
    Cdc42, we generated myeloid-restricted Cdc42 knock-out mice. Cdc42-deficient macrophages
    exhibited rapid phagocytic cup kinetics, but reduced particle clearance, which
    could be explained by the marked rounded-up morphology of these cells. Macrophages
    lacking Myo10, thought to act downstream of Cdc42, had normal morphology, motility,
    and phagocytic cup formation, but displayed markedly reduced filopodia formation.
    In conclusion, live-cell imaging revealed multiple mechanisms involving macrophage
    filopodia in particle capture and engulfment. Cdc42 is not critical for filopodia
    or phagocytic cup formation, but plays a key role in driving macrophage lamellipodial
    spreading.
article_processing_charge: No
article_type: original
author:
- first_name: Markus
  full_name: Horsthemke, Markus
  last_name: Horsthemke
- first_name: Anne
  full_name: Bachg, Anne
  last_name: Bachg
- first_name: Katharina
  full_name: Groll, Katharina
  last_name: Groll
- first_name: Sven
  full_name: Moyzio, Sven
  last_name: Moyzio
- first_name: Barbara
  full_name: Müther, Barbara
  last_name: Müther
- first_name: Sandra
  full_name: Hemkemeyer, Sandra
  last_name: Hemkemeyer
- first_name: Roland
  full_name: Wedlich Söldner, Roland
  last_name: Wedlich Söldner
- first_name: Michael K
  full_name: Sixt, Michael K
  id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
  last_name: Sixt
  orcid: 0000-0002-6620-9179
- first_name: Sebastian
  full_name: Tacke, Sebastian
  last_name: Tacke
- first_name: Martin
  full_name: Bähler, Martin
  last_name: Bähler
- first_name: Peter
  full_name: Hanley, Peter
  last_name: Hanley
citation:
  ama: Horsthemke M, Bachg A, Groll K, et al. Multiple roles of filopodial dynamics
    in particle capture and phagocytosis and phenotypes of Cdc42 and Myo10 deletion.
    <i>Journal of Biological Chemistry</i>. 2017;292(17):7258-7273. doi:<a href="https://doi.org/10.1074/jbc.M116.766923">10.1074/jbc.M116.766923</a>
  apa: Horsthemke, M., Bachg, A., Groll, K., Moyzio, S., Müther, B., Hemkemeyer, S.,
    … Hanley, P. (2017). Multiple roles of filopodial dynamics in particle capture
    and phagocytosis and phenotypes of Cdc42 and Myo10 deletion. <i>Journal of Biological
    Chemistry</i>. American Society for Biochemistry and Molecular Biology. <a href="https://doi.org/10.1074/jbc.M116.766923">https://doi.org/10.1074/jbc.M116.766923</a>
  chicago: Horsthemke, Markus, Anne Bachg, Katharina Groll, Sven Moyzio, Barbara Müther,
    Sandra Hemkemeyer, Roland Wedlich Söldner, et al. “Multiple Roles of Filopodial
    Dynamics in Particle Capture and Phagocytosis and Phenotypes of Cdc42 and Myo10
    Deletion.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry
    and Molecular Biology, 2017. <a href="https://doi.org/10.1074/jbc.M116.766923">https://doi.org/10.1074/jbc.M116.766923</a>.
  ieee: M. Horsthemke <i>et al.</i>, “Multiple roles of filopodial dynamics in particle
    capture and phagocytosis and phenotypes of Cdc42 and Myo10 deletion,” <i>Journal
    of Biological Chemistry</i>, vol. 292, no. 17. American Society for Biochemistry
    and Molecular Biology, pp. 7258–7273, 2017.
  ista: Horsthemke M, Bachg A, Groll K, Moyzio S, Müther B, Hemkemeyer S, Wedlich
    Söldner R, Sixt MK, Tacke S, Bähler M, Hanley P. 2017. Multiple roles of filopodial
    dynamics in particle capture and phagocytosis and phenotypes of Cdc42 and Myo10
    deletion. Journal of Biological Chemistry. 292(17), 7258–7273.
  mla: Horsthemke, Markus, et al. “Multiple Roles of Filopodial Dynamics in Particle
    Capture and Phagocytosis and Phenotypes of Cdc42 and Myo10 Deletion.” <i>Journal
    of Biological Chemistry</i>, vol. 292, no. 17, American Society for Biochemistry
    and Molecular Biology, 2017, pp. 7258–73, doi:<a href="https://doi.org/10.1074/jbc.M116.766923">10.1074/jbc.M116.766923</a>.
  short: M. Horsthemke, A. Bachg, K. Groll, S. Moyzio, B. Müther, S. Hemkemeyer, R.
    Wedlich Söldner, M.K. Sixt, S. Tacke, M. Bähler, P. Hanley, Journal of Biological
    Chemistry 292 (2017) 7258–7273.
date_created: 2018-12-11T11:47:49Z
date_published: 2017-04-28T00:00:00Z
date_updated: 2025-09-11T07:03:17Z
day: '28'
ddc:
- '570'
department:
- _id: MiSi
doi: 10.1074/jbc.M116.766923
external_id:
  isi:
  - '000400478300035'
file:
- access_level: open_access
  checksum: d488162874326a4bb056065fa549dc4a
  content_type: application/pdf
  creator: dernst
  date_created: 2019-10-24T15:25:42Z
  date_updated: 2020-07-14T12:47:37Z
  file_id: '6971'
  file_name: 2017_JBC_Horsthemke.pdf
  file_size: 5647880
  relation: main_file
file_date_updated: 2020-07-14T12:47:37Z
fulldoi: https://doi.org/10.1074/jbc.M116.766923
has_accepted_license: '1'
intvolume: '       292'
isi: 1
issue: '17'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 7258 - 7273
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '7059'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Multiple roles of filopodial dynamics in particle capture and phagocytosis
  and phenotypes of Cdc42 and Myo10 deletion
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 292
year: '2017'
...
---
_id: '6298'
abstract:
- lang: eng
  text: Tumor necrosis factor-stimulated gene-6 (TSG-6) is a hyalu-ronan (HA)-binding
    protein that plays important roles ininflammation and ovulation. TSG-6-mediated
    cross-linking ofHA has been proposed as a functional mechanism (e.g.for regu-lating
    leukocyte adhesion), but direct evidence for cross-linkingis lacking, and we know
    very little about its impact on HA ultra-structure. Here we used films of polymeric
    and oligomeric HAchains, end-grafted to a solid support, and a combination ofsurface-sensitive
    biophysical techniques to quantify the bindingof TSG-6 into HA films and to correlate
    binding to morpholog-ical changes. We find that full-length TSG-6 binds with pro-nounced
    positive cooperativity and demonstrate that it cancross-link HA at physiologically
    relevant concentrations. Ourdata indicate that cooperative binding of full-length
    TSG-6arises from HA-induced protein oligomerization and that theTSG-6 oligomers
    act as cross-linkers. In contrast, the HA-bind-ing domain of TSG-6 (the Link module)
    alone binds withoutpositive cooperativity and weaker than the full-length protein.Both
    the Link module and full-length TSG-6 condensed andrigidified HA films, and the
    degree of condensation scaled withthe affinity between the TSG-6 constructs and
    HA. We proposethat condensation is the result of protein-mediated HA cross-linking.
    Our findings firmly establish that TSG-6 is a potent HAcross-linking agent and
    might hence have important implica-tions for the mechanistic understanding of
    the biological func-tion of TSG-6 (e.g.in inflammation).
author:
- first_name: Natalia
  full_name: Baranova, Natalia
  id: 38661662-F248-11E8-B48F-1D18A9856A87
  last_name: Baranova
  orcid: 0000-0002-3086-9124
- first_name: Erik
  full_name: Nilebäck, Erik
  last_name: Nilebäck
- first_name: F. Michael
  full_name: Haller, F. Michael
  last_name: Haller
- first_name: David C.
  full_name: Briggs, David C.
  last_name: Briggs
- first_name: Sofia
  full_name: Svedhem, Sofia
  last_name: Svedhem
- first_name: Anthony J.
  full_name: Day, Anthony J.
  last_name: Day
- first_name: Ralf P.
  full_name: Richter, Ralf P.
  last_name: Richter
citation:
  ama: Baranova NS, Nilebäck E, Haller FM, et al. The inflammation-associated protein
    TSG-6 cross-links hyaluronan via hyaluronan-induced TSG-6 oligomers. <i>Journal
    of Biological Chemistry</i>. 2011;286(29):25675-25686. doi:<a href="https://doi.org/10.1074/jbc.m111.247395">10.1074/jbc.m111.247395</a>
  apa: Baranova, N. S., Nilebäck, E., Haller, F. M., Briggs, D. C., Svedhem, S., Day,
    A. J., &#38; Richter, R. P. (2011). The inflammation-associated protein TSG-6
    cross-links hyaluronan via hyaluronan-induced TSG-6 oligomers. <i>Journal of Biological
    Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href="https://doi.org/10.1074/jbc.m111.247395">https://doi.org/10.1074/jbc.m111.247395</a>
  chicago: Baranova, Natalia S., Erik Nilebäck, F. Michael Haller, David C. Briggs,
    Sofia Svedhem, Anthony J. Day, and Ralf P. Richter. “The Inflammation-Associated
    Protein TSG-6 Cross-Links Hyaluronan via Hyaluronan-Induced TSG-6 Oligomers.”
    <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38;
    Molecular Biology, 2011. <a href="https://doi.org/10.1074/jbc.m111.247395">https://doi.org/10.1074/jbc.m111.247395</a>.
  ieee: N. S. Baranova <i>et al.</i>, “The inflammation-associated protein TSG-6 cross-links
    hyaluronan via hyaluronan-induced TSG-6 oligomers,” <i>Journal of Biological Chemistry</i>,
    vol. 286, no. 29. American Society for Biochemistry &#38; Molecular Biology, pp.
    25675–25686, 2011.
  ista: Baranova NS, Nilebäck E, Haller FM, Briggs DC, Svedhem S, Day AJ, Richter
    RP. 2011. The inflammation-associated protein TSG-6 cross-links hyaluronan via
    hyaluronan-induced TSG-6 oligomers. Journal of Biological Chemistry. 286(29),
    25675–25686.
  mla: Baranova, Natalia S., et al. “The Inflammation-Associated Protein TSG-6 Cross-Links
    Hyaluronan via Hyaluronan-Induced TSG-6 Oligomers.” <i>Journal of Biological Chemistry</i>,
    vol. 286, no. 29, American Society for Biochemistry &#38; Molecular Biology, 2011,
    pp. 25675–86, doi:<a href="https://doi.org/10.1074/jbc.m111.247395">10.1074/jbc.m111.247395</a>.
  short: N.S. Baranova, E. Nilebäck, F.M. Haller, D.C. Briggs, S. Svedhem, A.J. Day,
    R.P. Richter, Journal of Biological Chemistry 286 (2011) 25675–25686.
date_created: 2019-04-11T20:57:43Z
date_published: 2011-07-22T00:00:00Z
date_updated: 2021-01-12T08:06:58Z
day: '22'
doi: 10.1074/jbc.m111.247395
extern: '1'
fulldoi: https://doi.org/10.1074/jbc.m111.247395
intvolume: '       286'
issue: '29'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: http://www.jbc.org/content/286/29/25675.full.pdf
month: '07'
oa: 1
oa_version: Published Version
page: 25675-25686
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
  - 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: The inflammation-associated protein TSG-6 cross-links hyaluronan via hyaluronan-induced
  TSG-6 oligomers
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 286
year: '2011'
...
---
_id: '8473'
abstract:
- lang: eng
  text: β2-microglobulin (β2m), the light chain of class I major histocompatibility
    complex, is responsible for the dialysis-related amyloidosis and, in patients
    undergoing long term dialysis, the full-length and chemically unmodified β2m converts
    into amyloid fibrils. The protein, belonging to the immunoglobulin superfamily,
    in common to other members of this family, experiences during its folding a long-lived
    intermediate associated to the trans-to-cis isomerization of Pro-32 that has been
    addressed as the precursor of the amyloid fibril formation. In this respect, previous
    studies on the W60G β2m mutant, showing that the lack of Trp-60 prevents fibril
    formation in mild aggregating condition, prompted us to reinvestigate the refolding
    kinetics of wild type and W60G β2m at atomic resolution by real-time NMR. The
    analysis, conducted at ambient temperature by the band selective flip angle short
    transient real-time two-dimensional NMR techniques and probing the β2m states
    every 15 s, revealed a more complex folding energy landscape than previously reported
    for wild type β2m, involving more than a single intermediate species, and shedding
    new light into the fibrillogenic pathway. Moreover, a significant difference in
    the kinetic scheme previously characterized by optical spectroscopic methods was
    discovered for the W60G β2m mutant.
article_processing_charge: No
article_type: original
author:
- first_name: Alessandra
  full_name: Corazza, Alessandra
  last_name: Corazza
- first_name: Enrico
  full_name: Rennella, Enrico
  last_name: Rennella
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Maria Chiara
  full_name: Mimmi, Maria Chiara
  last_name: Mimmi
- first_name: Thomas
  full_name: Cutuil, Thomas
  last_name: Cutuil
- first_name: Sara
  full_name: Raimondi, Sara
  last_name: Raimondi
- first_name: Sofia
  full_name: Giorgetti, Sofia
  last_name: Giorgetti
- first_name: Federico
  full_name: Fogolari, Federico
  last_name: Fogolari
- first_name: Paolo
  full_name: Viglino, Paolo
  last_name: Viglino
- first_name: Lucio
  full_name: Frydman, Lucio
  last_name: Frydman
- first_name: Maayan
  full_name: Gal, Maayan
  last_name: Gal
- first_name: Vittorio
  full_name: Bellotti, Vittorio
  last_name: Bellotti
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
- first_name: Gennaro
  full_name: Esposito, Gennaro
  last_name: Esposito
citation:
  ama: Corazza A, Rennella E, Schanda P, et al. Native-unlike long-lived intermediates
    along the folding pathway of the amyloidogenic protein β2-Microglobulin revealed
    by real-time two-dimensional NMR. <i>Journal of Biological Chemistry</i>. 2010;285(8):5827-5835.
    doi:<a href="https://doi.org/10.1074/jbc.m109.061168">10.1074/jbc.m109.061168</a>
  apa: Corazza, A., Rennella, E., Schanda, P., Mimmi, M. C., Cutuil, T., Raimondi,
    S., … Esposito, G. (2010). Native-unlike long-lived intermediates along the folding
    pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional
    NMR. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry
    &#38; Molecular Biology. <a href="https://doi.org/10.1074/jbc.m109.061168">https://doi.org/10.1074/jbc.m109.061168</a>
  chicago: Corazza, Alessandra, Enrico Rennella, Paul Schanda, Maria Chiara Mimmi,
    Thomas Cutuil, Sara Raimondi, Sofia Giorgetti, et al. “Native-Unlike Long-Lived
    Intermediates along the Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin
    Revealed by Real-Time Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry &#38; Molecular Biology, 2010. <a href="https://doi.org/10.1074/jbc.m109.061168">https://doi.org/10.1074/jbc.m109.061168</a>.
  ieee: A. Corazza <i>et al.</i>, “Native-unlike long-lived intermediates along the
    folding pathway of the amyloidogenic protein β2-Microglobulin revealed by real-time
    two-dimensional NMR,” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8.
    American Society for Biochemistry &#38; Molecular Biology, pp. 5827–5835, 2010.
  ista: Corazza A, Rennella E, Schanda P, Mimmi MC, Cutuil T, Raimondi S, Giorgetti
    S, Fogolari F, Viglino P, Frydman L, Gal M, Bellotti V, Brutscher B, Esposito
    G. 2010. Native-unlike long-lived intermediates along the folding pathway of the
    amyloidogenic protein β2-Microglobulin revealed by real-time two-dimensional NMR.
    Journal of Biological Chemistry. 285(8), 5827–5835.
  mla: Corazza, Alessandra, et al. “Native-Unlike Long-Lived Intermediates along the
    Folding Pathway of the Amyloidogenic Protein Β2-Microglobulin Revealed by Real-Time
    Two-Dimensional NMR.” <i>Journal of Biological Chemistry</i>, vol. 285, no. 8,
    American Society for Biochemistry &#38; Molecular Biology, 2010, pp. 5827–35,
    doi:<a href="https://doi.org/10.1074/jbc.m109.061168">10.1074/jbc.m109.061168</a>.
  short: A. Corazza, E. Rennella, P. Schanda, M.C. Mimmi, T. Cutuil, S. Raimondi,
    S. Giorgetti, F. Fogolari, P. Viglino, L. Frydman, M. Gal, V. Bellotti, B. Brutscher,
    G. Esposito, Journal of Biological Chemistry 285 (2010) 5827–5835.
date_created: 2020-09-18T10:11:23Z
date_published: 2010-02-19T00:00:00Z
date_updated: 2021-01-12T08:19:31Z
day: '19'
doi: 10.1074/jbc.m109.061168
extern: '1'
fulldoi: https://doi.org/10.1074/jbc.m109.061168
intvolume: '       285'
issue: '8'
keyword:
- Cell Biology
- Biochemistry
- Molecular Biology
language:
- iso: eng
month: '02'
oa_version: None
page: 5827-5835
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
  - 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic
  protein β2-Microglobulin revealed by real-time two-dimensional NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 285
year: '2010'
...
---
OA_type: closed access
_id: '2307'
abstract:
- lang: eng
  text: The human norepinephrine (NE) transporter (hNET) attenuates neuronal signaling
    by rapid NE clearance from the synaptic cleft, and NET is a target for cocaine
    and amphetamines as well as therapeutics for depression, obsessive-compulsive
    disorder, and post-traumatic stress disorder. In spite of its central importance
    in the nervous system, little is known about how NET substrates, such as NE, 1-methyl-4-tetrahydropyridinium
    (MPP+), or amphetamine, interact with NET at the molecular level. Nor do we understand
    the mechanisms behind the transport rate. Previously we introduced a fluorescent
    substrate similar to MPP+, which allowed separate and simultaneous binding and
    transport measurement (Schwartz, J. W., Blakely, R. D., and DeFelice, L. J. (2003)
    J. Biol. Chem. 278, 9768-9777). Here we use this substrate, 4-(4-(dimethylamino)styrl)-N-methyl-pyridinium
    (ASP+), in combination with green fluorescent protein-tagged hNETs to measure
    substrate-transporter stoichiometry and substrate binding kinetics. Calibrated
    confocal microscopy and fluorescence correlation spectroscopy reveal that hNETs,
    which are homo-multimers, bind one substrate molecule per transporter subunit.
    Substrate residence at the transporter, obtained from rapid on-off kinetics revealed
    in fluorescence correlation spectroscopy, is 526 μs. Substrate residence obtained
    by infinite dilution is 1000 times slower. This novel examination of substrate-transporter
    kinetics indicates that a single ASP + molecule binds and unbinds thousands of
    times before being transported or ultimately dissociated from hNET. Calibrated
    fluorescent images combined with mass spectroscopy give a transport rate of 0.06
    ASP +/hNET-protein/s, thus 36,000 on-off binding events (and 36 actual departures)
    occur for one transport event. Therefore binding has a low probability of resulting
    in transport. We interpret these data to mean that inefficient binding could contribute
    to slow transport rates.
article_processing_charge: No
article_type: original
author:
- first_name: Joel
  full_name: Schwartz, Joel
  last_name: Schwartz
- first_name: Gaia
  full_name: Novarino, Gaia
  id: 3E57A680-F248-11E8-B48F-1D18A9856A87
  last_name: Novarino
  orcid: 0000-0002-7673-7178
- first_name: David
  full_name: Piston, David
  last_name: Piston
- first_name: Louis
  full_name: Defelice, Louis
  last_name: Defelice
citation:
  ama: Schwartz J, Novarino G, Piston D, Defelice L. Substrate binding stoichiometry
    and kinetics of the norepinephrine transporter. <i>Journal of Biological Chemistry</i>.
    2005;280(19):19177-19184. doi:<a href="https://doi.org/10.1074/jbc.M412923200">10.1074/jbc.M412923200</a>
  apa: Schwartz, J., Novarino, G., Piston, D., &#38; Defelice, L. (2005). Substrate
    binding stoichiometry and kinetics of the norepinephrine transporter. <i>Journal
    of Biological Chemistry</i>. American Society for Biochemistry and Molecular Biology.
    <a href="https://doi.org/10.1074/jbc.M412923200">https://doi.org/10.1074/jbc.M412923200</a>
  chicago: Schwartz, Joel, Gaia Novarino, David Piston, and Louis Defelice. “Substrate
    Binding Stoichiometry and Kinetics of the Norepinephrine Transporter.” <i>Journal
    of Biological Chemistry</i>. American Society for Biochemistry and Molecular Biology,
    2005. <a href="https://doi.org/10.1074/jbc.M412923200">https://doi.org/10.1074/jbc.M412923200</a>.
  ieee: J. Schwartz, G. Novarino, D. Piston, and L. Defelice, “Substrate binding stoichiometry
    and kinetics of the norepinephrine transporter,” <i>Journal of Biological Chemistry</i>,
    vol. 280, no. 19. American Society for Biochemistry and Molecular Biology, pp.
    19177–19184, 2005.
  ista: Schwartz J, Novarino G, Piston D, Defelice L. 2005. Substrate binding stoichiometry
    and kinetics of the norepinephrine transporter. Journal of Biological Chemistry.
    280(19), 19177–19184.
  mla: Schwartz, Joel, et al. “Substrate Binding Stoichiometry and Kinetics of the
    Norepinephrine Transporter.” <i>Journal of Biological Chemistry</i>, vol. 280,
    no. 19, American Society for Biochemistry and Molecular Biology, 2005, pp. 19177–84,
    doi:<a href="https://doi.org/10.1074/jbc.M412923200">10.1074/jbc.M412923200</a>.
  short: J. Schwartz, G. Novarino, D. Piston, L. Defelice, Journal of Biological Chemistry
    280 (2005) 19177–19184.
date_created: 2018-12-11T11:56:54Z
date_published: 2005-05-13T00:00:00Z
date_updated: 2026-08-07T09:25:18Z
day: '13'
doi: 10.1074/jbc.M412923200
extern: '1'
external_id:
  pmid:
  - '15757904'
fulldoi: https://doi.org/10.1074/jbc.M412923200
intvolume: '       280'
issue: '19'
language:
- iso: eng
month: '05'
oa_version: None
page: 19177 - 19184
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '4619'
status: public
title: Substrate binding stoichiometry and kinetics of the norepinephrine transporter
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 280
year: '2005'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '2633'
abstract:
- lang: eng
  text: The modulation of calcium channels by metabotropic glutamate receptors (mGluRs)
    is a key event in the fine-tuning of neurotransmitter release. Here we report
    that, in cerebrocortical nerve terminals of adult rats, the inhibition of glutamate
    release is mediated by mGluR7. In this preparation, the major component of glutamate
    release is supported by P/Q-type Ca2+ channels (72.7%). However, mGluR7 selectively
    reduced the release component that is associated with N-type Ca2+ channels (29.9%).
    Inhibition of P/Q channels by mGluR7 is not masked by the higher efficiency of
    these channels in driving glutamate release when compared with N-type channels.
    Thus, activation of mGluR7 failed to reduce the release associated with P/Q channels
    when the extracellular calcium concentration, ([Ca2+]o), was reduced from 1.3
    to 0.5 mM. Through Ca2+ imaging, we show that Ca2+ channels are distributed in
    a heterogeneous manner in individual nerve terminals. Indeed, in this preparation,
    nerve terminals were observed that contain N-type (31.1%; conotoxin GVIA-sensitive)
    or P/Q-type (64.3%; agatoxin IVA-sensitive) channels or that were insensitive
    to these two toxins (4.6%). Interestingly, the great majority of the responses
    to L-AP4 (95.4%) were observed in nerve terminals containing N-type channels.
    This specific co-localization of mGluR7 and N-type Ca2+-channels could explain
    the failure of the receptor to inhibit the P/Q channel-associated release component
    and also reveal the existence of specific targeting mechanisms to localize the
    two proteins in the same nerve terminal subset.
article_processing_charge: No
article_type: original
author:
- first_name: Carmelo
  full_name: Millán, Carmelo
  last_name: Millán
- first_name: Enrique
  full_name: Castro, Enrique
  last_name: Castro
- first_name: Magdalena
  full_name: Torres, Magdalena
  last_name: Torres
- first_name: Ryuichi
  full_name: Shigemoto, Ryuichi
  id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
  last_name: Shigemoto
  orcid: 0000-0001-8761-9444
- first_name: José
  full_name: Sánchez Prieto, José
  last_name: Sánchez Prieto
citation:
  ama: Millán C, Castro E, Torres M, Shigemoto R, Sánchez Prieto J. Co-expression
    of metabotropic glutamate receptor 7 and N-type Ca2+ channels in single cerebrocortical
    nerve terminals of adult rats. <i>Journal of Biological Chemistry</i>. 2003;278(26):23955-23962.
    doi:<a href="https://doi.org/10.1074/jbc.M211471200">10.1074/jbc.M211471200</a>
  apa: Millán, C., Castro, E., Torres, M., Shigemoto, R., &#38; Sánchez Prieto, J.
    (2003). Co-expression of metabotropic glutamate receptor 7 and N-type Ca2+ channels
    in single cerebrocortical nerve terminals of adult rats. <i>Journal of Biological
    Chemistry</i>. Elsevier. <a href="https://doi.org/10.1074/jbc.M211471200">https://doi.org/10.1074/jbc.M211471200</a>
  chicago: Millán, Carmelo, Enrique Castro, Magdalena Torres, Ryuichi Shigemoto, and
    José Sánchez Prieto. “Co-Expression of Metabotropic Glutamate Receptor 7 and N-Type
    Ca2+ Channels in Single Cerebrocortical Nerve Terminals of Adult Rats.” <i>Journal
    of Biological Chemistry</i>. Elsevier, 2003. <a href="https://doi.org/10.1074/jbc.M211471200">https://doi.org/10.1074/jbc.M211471200</a>.
  ieee: C. Millán, E. Castro, M. Torres, R. Shigemoto, and J. Sánchez Prieto, “Co-expression
    of metabotropic glutamate receptor 7 and N-type Ca2+ channels in single cerebrocortical
    nerve terminals of adult rats,” <i>Journal of Biological Chemistry</i>, vol. 278,
    no. 26. Elsevier, pp. 23955–23962, 2003.
  ista: Millán C, Castro E, Torres M, Shigemoto R, Sánchez Prieto J. 2003. Co-expression
    of metabotropic glutamate receptor 7 and N-type Ca2+ channels in single cerebrocortical
    nerve terminals of adult rats. Journal of Biological Chemistry. 278(26), 23955–23962.
  mla: Millán, Carmelo, et al. “Co-Expression of Metabotropic Glutamate Receptor 7
    and N-Type Ca2+ Channels in Single Cerebrocortical Nerve Terminals of Adult Rats.”
    <i>Journal of Biological Chemistry</i>, vol. 278, no. 26, Elsevier, 2003, pp.
    23955–62, doi:<a href="https://doi.org/10.1074/jbc.M211471200">10.1074/jbc.M211471200</a>.
  short: C. Millán, E. Castro, M. Torres, R. Shigemoto, J. Sánchez Prieto, Journal
    of Biological Chemistry 278 (2003) 23955–23962.
date_created: 2018-12-11T11:58:47Z
date_published: 2003-07-27T00:00:00Z
date_updated: 2026-05-22T10:29:51Z
day: '27'
doi: 10.1074/jbc.M211471200
extern: '1'
external_id:
  pmid:
  - '12692128 '
fulldoi: https://doi.org/10.1074/jbc.M211471200
intvolume: '       278'
issue: '26'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1074/jbc.M211471200
month: '07'
oa: 1
oa_version: Published Version
page: 23955 - 23962
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: Elsevier
publist_id: '4265'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Co-expression of metabotropic glutamate receptor 7 and N-type Ca2+ channels
  in single cerebrocortical nerve terminals of adult rats
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 278
year: '2003'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '1959'
abstract:
- lang: eng
  text: 'The molecular organization of bacterial NADH: ubiquinone oxidoreductase (complex
    I or NDH-1) is not established, apart from a rough separation into dehydrogenase,
    connecting and membrane domains. In this work, complex I was purified from Escherichia
    coli and fragmented by replacing dodecylmaltoside with other detergents. Exchange
    into decyl maltoside led to the removal of the hydrophobic subunit NuoL from the
    otherwise intact complex. Diheptanoyl phosphocholine led to the loss of NuoL and
    NuoM subunits, whereas other subunits remained in the complex. The presence of
    N,N-dimethyldodecylamine N-oxide or Triton X-100 led to further disruption of
    the membrane domain into fragments containing NuoL/M/N, NuoA/K/N, and NuoH/J subunits.
    Among the hydrophilic subunits, NuoCD was most readily dissociated from the complex,
    whereas NuoB was partially dissociated from the peripheral arm assembly in N,N-dimethyldodecylamine
    N-oxide. A model of subunit arrangement in bacterial complex I based on these
    data is proposed. Subunits NuoL and NuoM, which are homologous to antiporters
    and are implicated in proton pumping, are located at the distal end of the membrane
    arm, spatially separated from the redox centers of the peripheral arm. This is
    consistent with proposals that the mechanism of proton pumping by complex I is
    likely to involve long range conformational changes.'
acknowledgement: his work was supported by the Medical Research Council.
article_processing_charge: No
article_type: original
author:
- first_name: Peter
  full_name: Holt, Peter
  last_name: Holt
- first_name: David
  full_name: Morgan, David
  last_name: Morgan
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
citation:
  ama: 'Holt P, Morgan D, Sazanov LA. The location of NuoL and NuoM subunits in the
    membrane domain of the Escherichia coli Complex I: implications for the mechanism
    of proton pumping. <i>Journal of Biological Chemistry</i>. 2003;278(44):43114-43120.
    doi:<a href="https://doi.org/10.1074/jbc.M308247200">10.1074/jbc.M308247200</a>'
  apa: 'Holt, P., Morgan, D., &#38; Sazanov, L. A. (2003). The location of NuoL and
    NuoM subunits in the membrane domain of the Escherichia coli Complex I: implications
    for the mechanism of proton pumping. <i>Journal of Biological Chemistry</i>. American
    Society for Biochemistry and Molecular Biology. <a href="https://doi.org/10.1074/jbc.M308247200">https://doi.org/10.1074/jbc.M308247200</a>'
  chicago: 'Holt, Peter, David Morgan, and Leonid A Sazanov. “The Location of NuoL
    and NuoM Subunits in the Membrane Domain of the Escherichia Coli Complex I: Implications
    for the Mechanism of Proton Pumping.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry and Molecular Biology, 2003. <a href="https://doi.org/10.1074/jbc.M308247200">https://doi.org/10.1074/jbc.M308247200</a>.'
  ieee: 'P. Holt, D. Morgan, and L. A. Sazanov, “The location of NuoL and NuoM subunits
    in the membrane domain of the Escherichia coli Complex I: implications for the
    mechanism of proton pumping,” <i>Journal of Biological Chemistry</i>, vol. 278,
    no. 44. American Society for Biochemistry and Molecular Biology, pp. 43114–43120,
    2003.'
  ista: 'Holt P, Morgan D, Sazanov LA. 2003. The location of NuoL and NuoM subunits
    in the membrane domain of the Escherichia coli Complex I: implications for the
    mechanism of proton pumping. Journal of Biological Chemistry. 278(44), 43114–43120.'
  mla: 'Holt, Peter, et al. “The Location of NuoL and NuoM Subunits in the Membrane
    Domain of the Escherichia Coli Complex I: Implications for the Mechanism of Proton
    Pumping.” <i>Journal of Biological Chemistry</i>, vol. 278, no. 44, American Society
    for Biochemistry and Molecular Biology, 2003, pp. 43114–20, doi:<a href="https://doi.org/10.1074/jbc.M308247200">10.1074/jbc.M308247200</a>.'
  short: P. Holt, D. Morgan, L.A. Sazanov, Journal of Biological Chemistry 278 (2003)
    43114–43120.
date_created: 2018-12-11T11:54:55Z
date_published: 2003-10-31T00:00:00Z
date_updated: 2026-05-28T11:41:17Z
day: '31'
doi: 10.1074/jbc.M308247200
extern: '1'
external_id:
  pmid:
  - '12923180'
fulldoi: https://doi.org/10.1074/jbc.M308247200
intvolume: '       278'
issue: '44'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1074/jbc.M308247200
month: '10'
oa: 1
oa_version: Published Version
page: 43114 - 43120
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '5124'
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'The location of NuoL and NuoM subunits in the membrane domain of the Escherichia
  coli Complex I: implications for the mechanism of proton pumping'
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 278
year: '2003'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '1960'
abstract:
- lang: eng
  text: NADH-ubiquinone oxidoreductase (complex I or NDH-1) was purified from the
    BL21 strain of Escherichia coli using an improved procedure. The complex was effectively
    stabilized by addition of divalent cations and lipids, making the preparation
    suitable for structural studies. The ubiquinone reductase activity of the enzyme
    was fully restored by addition of native E. coli lipids. Two different two-dimensional
    crystal forms, with p2 and p3 symmetry, were obtained using lipids containing
    native E. coli extracts. Analysis of the crystals showed that they are formed
    by fully intact complex I in an L-shaped conformation. Activity assays and single
    particle analysis indicated that complex I maintains this structure in detergent
    solution and does not adopt a different conformation in the active state. Thus,
    we provide the first experimental evidence that complex I from E. coli has an
    L-shape in a lipid bilayer and confirm that this is also the case for the active
    enzyme in solution. This suggests strongly that bacterial complex I exists in
    an L-shaped conformation in vivo. Our results also indicate that native lipids
    play an important role in the activation, stabilization and, as a consequence,
    crystallization of purified complex I from E. coli.
article_processing_charge: No
article_type: original
author:
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
- first_name: Joe
  full_name: Carroll, Joe
  last_name: Carroll
- first_name: Peter
  full_name: Holt, Peter
  last_name: Holt
- first_name: Laurence
  full_name: Toime, Laurence
  last_name: Toime
- first_name: Ian
  full_name: Fearnley, Ian
  last_name: Fearnley
citation:
  ama: Sazanov LA, Carroll J, Holt P, Toime L, Fearnley I. A role for native lipids
    in the stabilization and two dimensional crystallization of the Escherichia coli
    NADH ubiquinone oxidoreductase (complex I). <i>Journal of Biological Chemistry</i>.
    2003;278(21):19483-19491. doi:<a href="https://doi.org/10.1074/jbc.M208959200">10.1074/jbc.M208959200</a>
  apa: Sazanov, L. A., Carroll, J., Holt, P., Toime, L., &#38; Fearnley, I. (2003).
    A role for native lipids in the stabilization and two dimensional crystallization
    of the Escherichia coli NADH ubiquinone oxidoreductase (complex I). <i>Journal
    of Biological Chemistry</i>. American Society for Biochemistry and Molecular Biology.
    <a href="https://doi.org/10.1074/jbc.M208959200">https://doi.org/10.1074/jbc.M208959200</a>
  chicago: Sazanov, Leonid A, Joe Carroll, Peter Holt, Laurence Toime, and Ian Fearnley.
    “A Role for Native Lipids in the Stabilization and Two Dimensional Crystallization
    of the Escherichia Coli NADH Ubiquinone Oxidoreductase (Complex I).” <i>Journal
    of Biological Chemistry</i>. American Society for Biochemistry and Molecular Biology,
    2003. <a href="https://doi.org/10.1074/jbc.M208959200">https://doi.org/10.1074/jbc.M208959200</a>.
  ieee: L. A. Sazanov, J. Carroll, P. Holt, L. Toime, and I. Fearnley, “A role for
    native lipids in the stabilization and two dimensional crystallization of the
    Escherichia coli NADH ubiquinone oxidoreductase (complex I),” <i>Journal of Biological
    Chemistry</i>, vol. 278, no. 21. American Society for Biochemistry and Molecular
    Biology, pp. 19483–19491, 2003.
  ista: Sazanov LA, Carroll J, Holt P, Toime L, Fearnley I. 2003. A role for native
    lipids in the stabilization and two dimensional crystallization of the Escherichia
    coli NADH ubiquinone oxidoreductase (complex I). Journal of Biological Chemistry.
    278(21), 19483–19491.
  mla: Sazanov, Leonid A., et al. “A Role for Native Lipids in the Stabilization and
    Two Dimensional Crystallization of the Escherichia Coli NADH Ubiquinone Oxidoreductase
    (Complex I).” <i>Journal of Biological Chemistry</i>, vol. 278, no. 21, American
    Society for Biochemistry and Molecular Biology, 2003, pp. 19483–91, doi:<a href="https://doi.org/10.1074/jbc.M208959200">10.1074/jbc.M208959200</a>.
  short: L.A. Sazanov, J. Carroll, P. Holt, L. Toime, I. Fearnley, Journal of Biological
    Chemistry 278 (2003) 19483–19491.
date_created: 2018-12-11T11:54:55Z
date_published: 2003-05-23T00:00:00Z
date_updated: 2026-05-28T11:49:06Z
day: '23'
doi: 10.1074/jbc.M208959200
extern: '1'
external_id:
  pmid:
  - '12637579'
fulldoi: https://doi.org/10.1074/jbc.M208959200
intvolume: '       278'
issue: '21'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1074/jbc.M208959200
month: '05'
oa: 1
oa_version: Published Version
page: 19483 - 19491
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '5125'
quality_controlled: '1'
scopus_import: '1'
status: public
title: A role for native lipids in the stabilization and two dimensional crystallization
  of the Escherichia coli NADH ubiquinone oxidoreductase (complex I)
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
volume: 278
year: '2003'
...
---
_id: '2614'
abstract:
- lang: eng
  text: Metabotropic glutamate receptors (mGluRs) from group III reduce glutamate
    release. Because these receptors reduce cAMP levels, we explored whether this
    signaling pathway contributes to release inhibition caused by mGluRs with low
    affinity for L-2-amino-4-phosphonobutyrate (L-AP4). In biochemical experiments
    with the population of cerebrocortical nerve terminals we find that L-AP4 (1 mM)
    inhibited the Ca2+dependent-evoked release of glutamate by 25%. This inhibitory
    effect was largely prevented by the pertussis toxin but was insensitive to inhibitors
    of protein kinase C bisindolylmaleimide and protein kinase A H-89. Furthermore,
    this inhibition was associated with reduction in N-type Ca2+ channel activity
    in the absence of any detectable change in cAMP levels. In the presence of forskolin,
    however, L-AP4 decreased the levels of cAMP. The activation of this additional
    signaling pathway was very efficient in counteracting the facilitation of glutamate
    release induced either by forskolin or the β-adrenergic receptor agonist isoproterenol.
    Imaging experiments to measure Ca2+ dynamics in single nerve terminals showed
    that L-AP4 strongly reduced the Ca2+ response in 28% of the nerve terminals. Moreover,
    immunochemical experiments showed that 25-35% of the nerve terminals that were
    immunopositive to synaptophysin were also immunoreactive to the low affinity L-AP4-sensitive
    mGluR7. Then, mGluR7 mediates the inhibition of glutamate release caused by 1
    mM L-AP4, primarily by a strong inhibition of Ca2+ channels, although high cAMP
    uncovers the receptor ability to decrease cAMP.
acknowledgement: We thank Dr. Enrique Castro from Las Palmas University for critical
  reading of the manuscript and M. Sefton for editorial assistance.
article_processing_charge: No
article_type: original
author:
- first_name: Carmelo
  full_name: Millán, Carmelo
  last_name: Millán
- first_name: Rafael
  full_name: Luján, Rafael
  last_name: Luján
- first_name: Ryuichi
  full_name: Shigemoto, Ryuichi
  id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
  last_name: Shigemoto
  orcid: 0000-0001-8761-9444
- first_name: José
  full_name: Sánchez Prieto, José
  last_name: Sánchez Prieto
citation:
  ama: Millán C, Luján R, Shigemoto R, Sánchez Prieto J. The inhibition of glutamate
    release by metabotropic glutamate receptor 7 affects both [Ca2+]c and cAMP. Evidence
    for a strong reduction of Ca2+ entry in single nerve terminals. <i>Journal of
    Biological Chemistry</i>. 2002;277(16):14092-14101. doi:<a href="https://doi.org/10.1074/jbc.M109044200">10.1074/jbc.M109044200</a>
  apa: Millán, C., Luján, R., Shigemoto, R., &#38; Sánchez Prieto, J. (2002). The
    inhibition of glutamate release by metabotropic glutamate receptor 7 affects both
    [Ca2+]c and cAMP. Evidence for a strong reduction of Ca2+ entry in single nerve
    terminals. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry
    and Molecular Biology. <a href="https://doi.org/10.1074/jbc.M109044200">https://doi.org/10.1074/jbc.M109044200</a>
  chicago: Millán, Carmelo, Rafael Luján, Ryuichi Shigemoto, and José Sánchez Prieto.
    “The Inhibition of Glutamate Release by Metabotropic Glutamate Receptor 7 Affects
    Both [Ca2+]c and CAMP. Evidence for a Strong Reduction of Ca2+ Entry in Single
    Nerve Terminals.” <i>Journal of Biological Chemistry</i>. American Society for
    Biochemistry and Molecular Biology, 2002. <a href="https://doi.org/10.1074/jbc.M109044200">https://doi.org/10.1074/jbc.M109044200</a>.
  ieee: C. Millán, R. Luján, R. Shigemoto, and J. Sánchez Prieto, “The inhibition
    of glutamate release by metabotropic glutamate receptor 7 affects both [Ca2+]c
    and cAMP. Evidence for a strong reduction of Ca2+ entry in single nerve terminals,”
    <i>Journal of Biological Chemistry</i>, vol. 277, no. 16. American Society for
    Biochemistry and Molecular Biology, pp. 14092–14101, 2002.
  ista: Millán C, Luján R, Shigemoto R, Sánchez Prieto J. 2002. The inhibition of
    glutamate release by metabotropic glutamate receptor 7 affects both [Ca2+]c and
    cAMP. Evidence for a strong reduction of Ca2+ entry in single nerve terminals.
    Journal of Biological Chemistry. 277(16), 14092–14101.
  mla: Millán, Carmelo, et al. “The Inhibition of Glutamate Release by Metabotropic
    Glutamate Receptor 7 Affects Both [Ca2+]c and CAMP. Evidence for a Strong Reduction
    of Ca2+ Entry in Single Nerve Terminals.” <i>Journal of Biological Chemistry</i>,
    vol. 277, no. 16, American Society for Biochemistry and Molecular Biology, 2002,
    pp. 14092–101, doi:<a href="https://doi.org/10.1074/jbc.M109044200">10.1074/jbc.M109044200</a>.
  short: C. Millán, R. Luján, R. Shigemoto, J. Sánchez Prieto, Journal of Biological
    Chemistry 277 (2002) 14092–14101.
date_created: 2018-12-11T11:58:41Z
date_published: 2002-04-19T00:00:00Z
date_updated: 2023-07-25T10:16:44Z
day: '19'
ddc:
- '570'
doi: 10.1074/jbc.M109044200
extern: '1'
external_id:
  pmid:
  - '11825890'
file:
- access_level: open_access
  checksum: 0290fcbbd9153ec654185b0c856f214c
  content_type: application/pdf
  creator: alisjak
  date_created: 2023-07-25T10:13:16Z
  date_updated: 2023-07-25T10:13:16Z
  file_id: '13309'
  file_name: 2002_JBC_Millan.pdf
  file_size: 2105520
  relation: main_file
  success: 1
file_date_updated: 2023-07-25T10:13:16Z
fulldoi: https://doi.org/10.1074/jbc.M109044200
has_accepted_license: '1'
intvolume: '       277'
issue: '16'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: 14092 - 14101
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '4284'
quality_controlled: '1'
scopus_import: '1'
status: public
title: The inhibition of glutamate release by metabotropic glutamate receptor 7 affects
  both [Ca2+]c and cAMP. Evidence for a strong reduction of Ca2+ entry in single nerve
  terminals
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 277
year: '2002'
...
---
_id: '2621'
abstract:
- lang: eng
  text: The release properties of glutamatergic nerve terminals are influenced by
    a number of factors, including the subtype of voltage-dependent calcium channel
    and the presence of presynaptic autoreceptors. Group III metabotropic glutamate
    receptors (mGluRs) mediate feedback inhibition of glutamate release by inhibiting
    Ca2+ channel activity. By imaging Ca2+ in preparations of cerebrocortical nerve
    terminals, we show that voltage-dependent Ca2+ channels are distributed in a heterogeneous
    manner in individual nerve terminals. Presynaptic terminals contained only N-type
    (47.5%; conotoxin GVIA-sensitive), P/Q-type (3.9%; agatoxin IVA-sensitive), or
    both N- and P/Q-type (42.6%) Ca2+ channels, although the remainder of the terminals
    (6.1%) were insensitive to these two toxins. In this preparation, two mGluRs with
    high and low affinity for L(+)-2-amino-4-phosphonobutyrate were identified by
    immunocytochemistry as mGluR4 and mGluR7, respectively. These receptors were responsible
    for 22.2 and 24.1% reduction of glutamate release, and they reduced the Ca2+ response
    in 24.4 and 30.3% of the nerve terminals, respectively. Interestingly, mGluR4
    was largely (73.7%) located in nerve terminals expressing both N- and P/Q-type
    Ca2+ channels, whereas mGluR7 was predominantly (69.9%) located in N-type Ca2+
    channel-expressing terminals. This specific coexpression of different group III
    mGluRs and Ca2+ channels may endow synaptic terminals with distinct release properties
    and reveals the existence of a high degree of presynaptic heterogeneity.
acknowledgement: We thank M. Sefton for editorial assistance.
article_processing_charge: No
article_type: original
author:
- first_name: Carmelo
  full_name: Millán, Carmelo
  last_name: Millán
- first_name: Rafael
  full_name: Luján, Rafael
  last_name: Luján
- first_name: Ryuichi
  full_name: Shigemoto, Ryuichi
  id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
  last_name: Shigemoto
  orcid: 0000-0001-8761-9444
- first_name: José
  full_name: Sánchez Prieto, José
  last_name: Sánchez Prieto
citation:
  ama: Millán C, Luján R, Shigemoto R, Sánchez Prieto J. Subtype-specific expression
    of Group III metabotropic glutamate receptors and Ca2+ channels in single nerve
    terminals. <i>Journal of Biological Chemistry</i>. 2002;277(49):47796-47803. doi:<a
    href="https://doi.org/10.1074/jbc.M207531200">10.1074/jbc.M207531200</a>
  apa: Millán, C., Luján, R., Shigemoto, R., &#38; Sánchez Prieto, J. (2002). Subtype-specific
    expression of Group III metabotropic glutamate receptors and Ca2+ channels in
    single nerve terminals. <i>Journal of Biological Chemistry</i>. American Society
    for Biochemistry and Molecular Biology. <a href="https://doi.org/10.1074/jbc.M207531200">https://doi.org/10.1074/jbc.M207531200</a>
  chicago: Millán, Carmelo, Rafael Luján, Ryuichi Shigemoto, and José Sánchez Prieto.
    “Subtype-Specific Expression of Group III Metabotropic Glutamate Receptors and
    Ca2+ Channels in Single Nerve Terminals.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry and Molecular Biology, 2002. <a href="https://doi.org/10.1074/jbc.M207531200">https://doi.org/10.1074/jbc.M207531200</a>.
  ieee: C. Millán, R. Luján, R. Shigemoto, and J. Sánchez Prieto, “Subtype-specific
    expression of Group III metabotropic glutamate receptors and Ca2+ channels in
    single nerve terminals,” <i>Journal of Biological Chemistry</i>, vol. 277, no.
    49. American Society for Biochemistry and Molecular Biology, pp. 47796–47803,
    2002.
  ista: Millán C, Luján R, Shigemoto R, Sánchez Prieto J. 2002. Subtype-specific expression
    of Group III metabotropic glutamate receptors and Ca2+ channels in single nerve
    terminals. Journal of Biological Chemistry. 277(49), 47796–47803.
  mla: Millán, Carmelo, et al. “Subtype-Specific Expression of Group III Metabotropic
    Glutamate Receptors and Ca2+ Channels in Single Nerve Terminals.” <i>Journal of
    Biological Chemistry</i>, vol. 277, no. 49, American Society for Biochemistry
    and Molecular Biology, 2002, pp. 47796–803, doi:<a href="https://doi.org/10.1074/jbc.M207531200">10.1074/jbc.M207531200</a>.
  short: C. Millán, R. Luján, R. Shigemoto, J. Sánchez Prieto, Journal of Biological
    Chemistry 277 (2002) 47796–47803.
date_created: 2018-12-11T11:58:43Z
date_published: 2002-12-02T00:00:00Z
date_updated: 2023-07-19T07:49:19Z
day: '02'
doi: 10.1074/jbc.M207531200
extern: '1'
external_id:
  pmid:
  - '12376542'
fulldoi: https://doi.org/10.1074/jbc.M207531200
intvolume: '       277'
issue: '49'
language:
- iso: eng
month: '12'
oa_version: Published Version
page: 47796 - 47803
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '4277'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Subtype-specific expression of Group III metabotropic glutamate receptors and
  Ca2+ channels in single nerve terminals
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 277
year: '2002'
...
---
_id: '13438'
abstract:
- lang: eng
  text: ICln is an ion channel identified by expression cloning using a cDNA library
    from Madin-Darby canine kidney cells. In all organisms tested so far, only one
    transcript for the ICln protein could be identified. Here we show that two splice
    variants of the ICln ion channel can be found in Caenorhabditis elegans. Moreover,
    we show that these two splice variants of the ICln channel protein, which we termed
    IClnN1 and IClnN2, can be functionally reconstituted and tested in an artificial
    lipid bilayer. In these experiments, the IClnN1-induced currents showed no voltage-dependent
    inactivation, whereas the IClnN2-induced currents fully inactivated at positive
    potentials. The molecular entity responsible for the voltage-dependent inactivation
    of IClnN2 is a cluster of positively charged amino acids encoded by exon 2a, which
    is absent in IClnN1. Our experiments suggest a mechanism of channel inactivation
    that is similar to the “ball and chain” model proposed for the Shaker potassium
    channel,i.e. a cluster of positively charged amino acids hinders ion permeation
    through the channel by a molecular and voltage-dependent interaction at the inner
    vestibulum of the pore. This hypothesis is supported by the finding that synthetic
    peptides with the same amino acid sequence as the positive cluster can transform
    the IClnN1-induced current to the current observed after reconstitution of IClnN2.
    Furthermore, we show that the nematode ICln gene is embedded in an operon harboring
    two additional genes, which we termed Nx and Ny. Co-reconstitution of Nx and IClnN2
    and functional analysis of the related currents revealed a functional interaction
    between the two proteins, as evidenced by the fact that the IClnN2-induced current
    in the presence of Nx was no longer voltage-sensitive. The experiments described
    indicate that the genome organization in nematodes allows an effective approach
    for the identification of functional partner proteins of ion channels.
acknowledgement: We are grateful to D. E. Clapham, E. Wöll, G. Meyer, and G. Botta
  for helpful discussion and/or reading of the manuscript. We also thank T. Stiernagle
  for providing the N2 strain of C. elegans and A. Wimmer and M. Frick for technical
  assistance
article_processing_charge: No
article_type: original
author:
- first_name: Johannes
  full_name: Fürst, Johannes
  last_name: Fürst
- first_name: Markus
  full_name: Ritter, Markus
  last_name: Ritter
- first_name: Jakob
  full_name: Rudzki, Jakob
  last_name: Rudzki
- first_name: Johann G
  full_name: Danzl, Johann G
  id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
  last_name: Danzl
  orcid: 0000-0001-8559-3973
- first_name: Martin
  full_name: Gschwentner, Martin
  last_name: Gschwentner
- first_name: Elke
  full_name: Scandella, Elke
  last_name: Scandella
- first_name: Martin
  full_name: Jakab, Martin
  last_name: Jakab
- first_name: Matthias
  full_name: König, Matthias
  last_name: König
- first_name: Bernhard
  full_name: Oehl, Bernhard
  last_name: Oehl
- first_name: Florian
  full_name: Lang, Florian
  last_name: Lang
- first_name: Peter
  full_name: Deetjen, Peter
  last_name: Deetjen
- first_name: Markus
  full_name: Paulmichl, Markus
  last_name: Paulmichl
citation:
  ama: Fürst J, Ritter M, Rudzki J, et al. ICln Ion channel splice variants in Caenorhabditis
    elegans. <i>Journal of Biological Chemistry</i>. 2002;277(6):4435-4445. doi:<a
    href="https://doi.org/10.1074/jbc.m107372200">10.1074/jbc.m107372200</a>
  apa: Fürst, J., Ritter, M., Rudzki, J., Danzl, J. G., Gschwentner, M., Scandella,
    E., … Paulmichl, M. (2002). ICln Ion channel splice variants in Caenorhabditis
    elegans. <i>Journal of Biological Chemistry</i>. Elsevier. <a href="https://doi.org/10.1074/jbc.m107372200">https://doi.org/10.1074/jbc.m107372200</a>
  chicago: Fürst, Johannes, Markus Ritter, Jakob Rudzki, Johann G Danzl, Martin Gschwentner,
    Elke Scandella, Martin Jakab, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
    Elegans.” <i>Journal of Biological Chemistry</i>. Elsevier, 2002. <a href="https://doi.org/10.1074/jbc.m107372200">https://doi.org/10.1074/jbc.m107372200</a>.
  ieee: J. Fürst <i>et al.</i>, “ICln Ion channel splice variants in Caenorhabditis
    elegans,” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6. Elsevier, pp.
    4435–4445, 2002.
  ista: Fürst J, Ritter M, Rudzki J, Danzl JG, Gschwentner M, Scandella E, Jakab M,
    König M, Oehl B, Lang F, Deetjen P, Paulmichl M. 2002. ICln Ion channel splice
    variants in Caenorhabditis elegans. Journal of Biological Chemistry. 277(6), 4435–4445.
  mla: Fürst, Johannes, et al. “ICln Ion Channel Splice Variants in Caenorhabditis
    Elegans.” <i>Journal of Biological Chemistry</i>, vol. 277, no. 6, Elsevier, 2002,
    pp. 4435–45, doi:<a href="https://doi.org/10.1074/jbc.m107372200">10.1074/jbc.m107372200</a>.
  short: J. Fürst, M. Ritter, J. Rudzki, J.G. Danzl, M. Gschwentner, E. Scandella,
    M. Jakab, M. König, B. Oehl, F. Lang, P. Deetjen, M. Paulmichl, Journal of Biological
    Chemistry 277 (2002) 4435–4445.
date_created: 2023-08-01T12:37:50Z
date_published: 2002-02-08T00:00:00Z
date_updated: 2023-08-01T12:55:54Z
day: '08'
ddc:
- '570'
doi: 10.1074/jbc.m107372200
extern: '1'
external_id:
  pmid:
  - '11706026'
file:
- access_level: open_access
  checksum: 13abe20f78eb37ab62beb006f62c69b7
  content_type: application/pdf
  creator: alisjak
  date_created: 2023-08-01T12:44:09Z
  date_updated: 2023-08-01T12:44:09Z
  file_id: '13439'
  file_name: 2002_JBC_Fuerst.pdf
  file_size: 798920
  relation: main_file
  success: 1
file_date_updated: 2023-08-01T12:44:09Z
fulldoi: https://doi.org/10.1074/jbc.m107372200
has_accepted_license: '1'
intvolume: '       277'
issue: '6'
keyword:
- Cell Biology
- Molecular Biology
- Biochemistry
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 4435-4445
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: ICln Ion channel splice variants in Caenorhabditis elegans
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 277
year: '2002'
...
---
_id: '3928'
abstract:
- lang: eng
  text: Regulated adhesion of leukocytes to the extracellular matrix is essential
    for transmigration of blood vessels and subsequent migration into the stroma of
    inflamed tissues. Although beta(2)-integrins play an indisputable role in adhesion
    of polymorphonuclear granulocytes (PMN) to endothelium, we show here that beta(1)-
    and beta(3)-integrins but not beta(2)-integrin are essential for the adhesion
    to and migration on extracellular matrix molecules of the endothelial cell basement
    membrane and subjacent interstitial matrix. Mouse wild type and beta(2)-integrin
    null PMN and the progranulocytic cell line 32DC13 were employed in in vitro adhesion
    and migration assays using extracellular matrix molecules expressed at sites of
    extravasation in vivo, in particular the endothelial cell laminins 8 and 10. Wild
    type and beta(2)-integrin null PMN showed the same pattern of ECM binding, indicating
    that beta(2)-integrins do not mediate specific adhesion of PMN to the extracellular
    matrix molecules tested; binding was observed to the interstitial matrix molecules,
    fibronectin and vitronectin, via integrins alpha(5)beta(1) and alpha(v)beta(3),
    respectively; to laminin 10 via alpha(6)beta(1); but not to laminins 1, 2, and
    8, collagen type I and IV, perlecan, or tenascin-C. PMN binding to laminins 1,
    2, and 8 could not be induced despite surface expression of functionally active
    integrin alpha(6)beta(1), a major laminin receptor, demonstrating that expression
    of alpha(6)beta(1) alone is insufficient for ligand binding and suggesting the
    involvement of accessory factors. Nevertheless, laminins 1, 8, and 10 supported
    PMN migration, indicating that differential cellular signaling via laminins is
    independent of the extent of adhesion. The data demonstrate that adhesive and
    nonadhesive interactions with components of the endothelial cell basement membrane
    and subjacent interstitium play decisive roles in controlling PMN movement into
    sites of inflammation and illustrate that beta(2)-integrins are not essential
    for such interactions.
acknowledgement: We thank Dr. T. Winkler for carrying out flow cytometry analysis,
  Dr. Simon Goodman for providing cyclic RGD peptides and helpful discussions, and
  Stefanie Karosi and Thomas Samson for critical review of the manuscript. This work
  would not have been possible without the expert technical assistance of Friederike
  Pausch.
article_processing_charge: No
article_type: original
author:
- first_name: Michael K
  full_name: Sixt, Michael K
  id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
  last_name: Sixt
  orcid: 0000-0002-6620-9179
- first_name: Rupert
  full_name: Hallmann, Rupert
  last_name: Hallmann
- first_name: Olaf
  full_name: Wendler, Olaf
  last_name: Wendler
- first_name: Karin
  full_name: Scharffetter Kochanek, Karin
  last_name: Scharffetter Kochanek
- first_name: Lydia
  full_name: Sorokin, Lydia
  last_name: Sorokin
citation:
  ama: Sixt MK, Hallmann R, Wendler O, Scharffetter Kochanek K, Sorokin L. Cell adhesion
    and migration properties of β2-integrin negative polymorphonuclear granulocytes
    on defined extracellular matrix molecules. Relevance for leukocyte extravasation.
    <i>Journal of Biological Chemistry</i>. 2001;276(22):18878-18887. doi:<a href="https://doi.org/10.1074/jbc.M010898200">10.1074/jbc.M010898200</a>
  apa: Sixt, M. K., Hallmann, R., Wendler, O., Scharffetter Kochanek, K., &#38; Sorokin,
    L. (2001). Cell adhesion and migration properties of β2-integrin negative polymorphonuclear
    granulocytes on defined extracellular matrix molecules. Relevance for leukocyte
    extravasation. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry
    and Molecular Biology. <a href="https://doi.org/10.1074/jbc.M010898200">https://doi.org/10.1074/jbc.M010898200</a>
  chicago: Sixt, Michael K, Rupert Hallmann, Olaf Wendler, Karin Scharffetter Kochanek,
    and Lydia Sorokin. “Cell Adhesion and Migration Properties of Β2-Integrin Negative
    Polymorphonuclear Granulocytes on Defined Extracellular Matrix Molecules. Relevance
    for Leukocyte Extravasation.” <i>Journal of Biological Chemistry</i>. American
    Society for Biochemistry and Molecular Biology, 2001. <a href="https://doi.org/10.1074/jbc.M010898200">https://doi.org/10.1074/jbc.M010898200</a>.
  ieee: M. K. Sixt, R. Hallmann, O. Wendler, K. Scharffetter Kochanek, and L. Sorokin,
    “Cell adhesion and migration properties of β2-integrin negative polymorphonuclear
    granulocytes on defined extracellular matrix molecules. Relevance for leukocyte
    extravasation,” <i>Journal of Biological Chemistry</i>, vol. 276, no. 22. American
    Society for Biochemistry and Molecular Biology, pp. 18878–18887, 2001.
  ista: Sixt MK, Hallmann R, Wendler O, Scharffetter Kochanek K, Sorokin L. 2001.
    Cell adhesion and migration properties of β2-integrin negative polymorphonuclear
    granulocytes on defined extracellular matrix molecules. Relevance for leukocyte
    extravasation. Journal of Biological Chemistry. 276(22), 18878–18887.
  mla: Sixt, Michael K., et al. “Cell Adhesion and Migration Properties of Β2-Integrin
    Negative Polymorphonuclear Granulocytes on Defined Extracellular Matrix Molecules.
    Relevance for Leukocyte Extravasation.” <i>Journal of Biological Chemistry</i>,
    vol. 276, no. 22, American Society for Biochemistry and Molecular Biology, 2001,
    pp. 18878–87, doi:<a href="https://doi.org/10.1074/jbc.M010898200">10.1074/jbc.M010898200</a>.
  short: M.K. Sixt, R. Hallmann, O. Wendler, K. Scharffetter Kochanek, L. Sorokin,
    Journal of Biological Chemistry 276 (2001) 18878–18887.
date_created: 2018-12-11T12:05:56Z
date_published: 2001-06-01T00:00:00Z
date_updated: 2023-05-11T12:54:06Z
day: '01'
doi: 10.1074/jbc.M010898200
extern: '1'
external_id:
  pmid:
  - '11278780'
fulldoi: https://doi.org/10.1074/jbc.M010898200
intvolume: '       276'
issue: '22'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.sciencedirect.com/science/article/pii/S0021925819670134?via%3Dihub
month: '06'
oa: 1
oa_version: Published Version
page: 18878 - 18887
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '2199'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cell adhesion and migration properties of β2-integrin negative polymorphonuclear
  granulocytes on defined extracellular matrix molecules. Relevance for leukocyte
  extravasation
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 276
year: '2001'
...
---
_id: '3149'
abstract:
- lang: eng
  text: The prohormone convertases (PCs) are an evolutionarily ancient group of proteases
    required for the maturation of neuropeptide and peptide hormone precursors. In
    Drosophila melanogaster, the homolog of prohormone convertase 2, dPC2 (amontillado),
    is required for normal hatching behavior, and immunoblotting data indicate that
    flies express 80- and 75-kDa forms of this protein. Because mouse PC2 (mPC2) requires
    7B2, a helper protein for productive maturation, we searched the fly data base
    for the 7B2 signature motif PPNPCP and identified an expressed sequence tag clone
    encoding the entire open reading frame for this protein. dPC2 and d7B2 cDNAs were
    subcloned into expression vectors for transfection into HEK-293 cells; mPC2 and
    rat 7B2 were used as controls. Although active mPC2 was detected in medium in
    the presence of either d7B2 or r7B2, dPC2 showed no proteolytic activity upon
    coexpression of either d7B2 or r7B2. Labeling experiments showed that dPC2 was
    synthesized but not secreted from HEK-293 cells. However, when dPC2 and either
    d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive
    dPC2 was secreted into the medium, coincident with the appearance of PC2 activity.
    Expression and secretion of dPC2 enzyme activity thus appears to require insect
    cell-specific posttranslational processing events. The significant differences
    in the cell biology of the insect and mammalian enzymes, with 7B2 absolutely required
    for secretion of dPC2 and zymogen conversion occurring intracellularly in the
    case of dPC2 but not mPC2, support the idea that the Drosophila enzyme has specific
    requirements for maturation and secretion that can be met only in insect cells.
acknowledgement: This work was supported by National Institutes of Health Grants DK49703
  (to I. L.), NS21749 (to P. H. T.), and GM39697 (to R. S. F.). The costs of publication
  of this article were defrayed in part by the payment of page charges. This article
  must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section
  1734 solely to indicate this fact. 10749852. We thank members of the Lindberg laboratory
  and Laurent Muller for helpful comments, Bin Tu for construction of the C. elegans
  PC2 expression vector, and Joelle Finley for assistance with cell culture.
article_processing_charge: No
article_type: original
author:
- first_name: Jae
  full_name: Hwang, Jae
  last_name: Hwang
- first_name: Daria E
  full_name: Siekhaus, Daria E
  id: 3D224B9E-F248-11E8-B48F-1D18A9856A87
  last_name: Siekhaus
  orcid: 0000-0001-8323-8353
- first_name: Robert
  full_name: Fuller, Robert
  last_name: Fuller
- first_name: Paul
  full_name: Taghert, Paul
  last_name: Taghert
- first_name: Iris
  full_name: Lindberg, Iris
  last_name: Lindberg
citation:
  ama: 'Hwang J, Siekhaus DE, Fuller R, Taghert P, Lindberg I. Interaction of Drosophila
    melanogaster prohormone convertase 2 and 7B2: Insect cell specific processing
    and secretion. <i>Journal of Biological Chemistry</i>. 2000;275(23):17886-17893.
    doi:<a href="https://doi.org/10.1074/jbc.M000032200 ">10.1074/jbc.M000032200 </a>'
  apa: 'Hwang, J., Siekhaus, D. E., Fuller, R., Taghert, P., &#38; Lindberg, I. (2000).
    Interaction of Drosophila melanogaster prohormone convertase 2 and 7B2: Insect
    cell specific processing and secretion. <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry and Molecular Biology. <a href="https://doi.org/10.1074/jbc.M000032200
    ">https://doi.org/10.1074/jbc.M000032200 </a>'
  chicago: 'Hwang, Jae, Daria E Siekhaus, Robert Fuller, Paul Taghert, and Iris Lindberg.
    “Interaction of Drosophila Melanogaster Prohormone Convertase 2 and 7B2: Insect
    Cell Specific Processing and Secretion.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry and Molecular Biology, 2000. <a href="https://doi.org/10.1074/jbc.M000032200
    ">https://doi.org/10.1074/jbc.M000032200 </a>.'
  ieee: 'J. Hwang, D. E. Siekhaus, R. Fuller, P. Taghert, and I. Lindberg, “Interaction
    of Drosophila melanogaster prohormone convertase 2 and 7B2: Insect cell specific
    processing and secretion,” <i>Journal of Biological Chemistry</i>, vol. 275, no.
    23. American Society for Biochemistry and Molecular Biology, pp. 17886–17893,
    2000.'
  ista: 'Hwang J, Siekhaus DE, Fuller R, Taghert P, Lindberg I. 2000. Interaction
    of Drosophila melanogaster prohormone convertase 2 and 7B2: Insect cell specific
    processing and secretion. Journal of Biological Chemistry. 275(23), 17886–17893.'
  mla: 'Hwang, Jae, et al. “Interaction of Drosophila Melanogaster Prohormone Convertase
    2 and 7B2: Insect Cell Specific Processing and Secretion.” <i>Journal of Biological
    Chemistry</i>, vol. 275, no. 23, American Society for Biochemistry and Molecular
    Biology, 2000, pp. 17886–93, doi:<a href="https://doi.org/10.1074/jbc.M000032200
    ">10.1074/jbc.M000032200 </a>.'
  short: J. Hwang, D.E. Siekhaus, R. Fuller, P. Taghert, I. Lindberg, Journal of Biological
    Chemistry 275 (2000) 17886–17893.
date_created: 2018-12-11T12:01:40Z
date_published: 2000-06-09T00:00:00Z
date_updated: 2023-05-03T08:47:13Z
day: '09'
doi: '10.1074/jbc.M000032200 '
extern: '1'
external_id:
  pmid:
  - '10749852'
fulldoi: 'https://doi.org/10.1074/jbc.M000032200 '
intvolume: '       275'
issue: '23'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.sciencedirect.com/science/article/pii/S0021925819833215?via%3Dihub
month: '06'
oa: 1
oa_version: Published Version
page: 17886 - 17893
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '3546'
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Interaction of Drosophila melanogaster prohormone convertase 2 and 7B2: Insect
  cell specific processing and secretion'
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 275
year: '2000'
...
---
_id: '4179'
abstract:
- lang: eng
  text: Neurotrophin-3 (NT-3) is a member of the neurotrophin gene family and is highly
    expressed in the developing rat cerebellum. Here we show that brain-derived neurotrophic
    factor (BDNF) increased by approximately 10-fold the NT-3 mRNA levels in cultured
    cerebellar granule neurons isolated from postnatal rats, whereas nerve growth
    factor (NGF) and NT-3 itself had no effect. The effect of BDNF was additive to
    that of triiodothyronine (T3), which also increased NT-3 mRNA in these neurons.
    The drug K252a inhibited the BDNF-mediated stimulation of NT-3 expression, suggesting
    an involvement of trkB receptors. Nuclear run-on experiments showed that BDNF
    enhanced NT-3 transcription, whereas the stability of NT-3 mRNA remained unchanged.
    The data presented are the first demonstration that one neurotrophin regulates
    the expression of another and provide evidence that NT-3 production in granule
    neurons is regulated by both BDNF and T3.
acknowledgement: We thank Dorothea Stratmann and Karin Angermayer for skillful technical
  assistance.
article_processing_charge: No
article_type: original
author:
- first_name: Axel
  full_name: Leingärtner, Axel
  last_name: Leingärtner
- first_name: Carl-Philipp J
  full_name: Heisenberg, Carl-Philipp J
  id: 39427864-F248-11E8-B48F-1D18A9856A87
  last_name: Heisenberg
  orcid: 0000-0002-0912-4566
- first_name: Roland
  full_name: Kolbeck, Roland
  last_name: Kolbeck
- first_name: Hans
  full_name: Thoenen, Hans
  last_name: Thoenen
- first_name: Dan
  full_name: Lindholm, Dan
  last_name: Lindholm
citation:
  ama: Leingärtner A, Heisenberg C-PJ, Kolbeck R, Thoenen H, Lindholm D. Brain-derived
    neurotrophic factor increases neurotrophin-3 expression in cerebellar granule
    neurons. <i>Journal of Biological Chemistry</i>. 1994;269(2):828-830. doi:<a href="https://doi.org/10.1016/s0021-9258(17)42186-7">10.1016/s0021-9258(17)42186-7</a>
  apa: Leingärtner, A., Heisenberg, C.-P. J., Kolbeck, R., Thoenen, H., &#38; Lindholm,
    D. (1994). Brain-derived neurotrophic factor increases neurotrophin-3 expression
    in cerebellar granule neurons. <i>Journal of Biological Chemistry</i>. American
    Society for Biochemistry and Molecular Biology. <a href="https://doi.org/10.1016/s0021-9258(17)42186-7">https://doi.org/10.1016/s0021-9258(17)42186-7</a>
  chicago: Leingärtner, Axel, Carl-Philipp J Heisenberg, Roland Kolbeck, Hans Thoenen,
    and Dan Lindholm. “Brain-Derived Neurotrophic Factor Increases Neurotrophin-3
    Expression in Cerebellar Granule Neurons.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry and Molecular Biology, 1994. <a href="https://doi.org/10.1016/s0021-9258(17)42186-7">https://doi.org/10.1016/s0021-9258(17)42186-7</a>.
  ieee: A. Leingärtner, C.-P. J. Heisenberg, R. Kolbeck, H. Thoenen, and D. Lindholm,
    “Brain-derived neurotrophic factor increases neurotrophin-3 expression in cerebellar
    granule neurons,” <i>Journal of Biological Chemistry</i>, vol. 269, no. 2. American
    Society for Biochemistry and Molecular Biology, pp. 828–830, 1994.
  ista: Leingärtner A, Heisenberg C-PJ, Kolbeck R, Thoenen H, Lindholm D. 1994. Brain-derived
    neurotrophic factor increases neurotrophin-3 expression in cerebellar granule
    neurons. Journal of Biological Chemistry. 269(2), 828–830.
  mla: Leingärtner, Axel, et al. “Brain-Derived Neurotrophic Factor Increases Neurotrophin-3
    Expression in Cerebellar Granule Neurons.” <i>Journal of Biological Chemistry</i>,
    vol. 269, no. 2, American Society for Biochemistry and Molecular Biology, 1994,
    pp. 828–30, doi:<a href="https://doi.org/10.1016/s0021-9258(17)42186-7">10.1016/s0021-9258(17)42186-7</a>.
  short: A. Leingärtner, C.-P.J. Heisenberg, R. Kolbeck, H. Thoenen, D. Lindholm,
    Journal of Biological Chemistry 269 (1994) 828–830.
date_created: 2018-12-11T12:07:25Z
date_published: 1994-01-14T00:00:00Z
date_updated: 2022-06-02T10:23:48Z
day: '14'
doi: 10.1016/s0021-9258(17)42186-7
extern: '1'
fulldoi: https://doi.org/10.1016/s0021-9258(17)42186-7
intvolume: '       269'
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.sciencedirect.com/science/article/pii/S0021925817421867?via%3Dihub
month: '01'
oa: 1
oa_version: None
page: 828 - 830
publication: Journal of Biological Chemistry
publication_identifier:
  eissn:
  - 1083-351X
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '1941'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Brain-derived neurotrophic factor increases neurotrophin-3 expression in cerebellar
  granule neurons
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 269
year: '1994'
...
---
_id: '2536'
abstract:
- lang: eng
  text: A cDNA clone for a new metabotropic glutamate receptor, termed mGluR6, was
    isolated from a rat retinal cDNA library by cross-hybridization with the previously
    isolated cDNA clone for a metabotropic glutamate receptor. The cloned mGluR6 subtype
    consists of 871 amino acid residues and exhibits a structural architecture common
    to the metabotropic receptor family, possessing a large extracellular domain preceding
    the seven putative membrane-spanning domains. mGluR6 shows the highest sequence
    similarity to mGluR4 among the metabotropic receptor subtypes and inhibits the
    forskolin- stimulated cyclic AMP accumulation in Chinese hamster ovary cells transfected
    with the cloned cDNA. mGluR6 potently reacts with L-2-amino-4- phosphonobutyrate
    (L-AP4) and L-serine-O-phosphate, and the potencies of these compounds are one
    order of magnitude greater than that of L-glutamate. Blot and in situ hybridization
    analyses indicated that mGluR6 mRNA is restrictedly expressed in the inner nuclear
    layer of the retina where ON- bipolar cells are distributed. The metabotropic
    receptor that responds strongly to L-AP4 and L-serine-O-phosphate in ON-bipolar
    cells is known to mediate glutamate synaptic transmission between photoreceptor
    cells and ON- bipolar cells. On the basis of the agonist selectivity of mGluR6
    and its specific expression in retinal cells, the physiological role of this receptor
    subtype in the visual system is discussed.
acknowledgement: "This work was supported in part by research grants from the Ministry
  of Education, Science and Culture of Japan, the Ministry of Health and Welfare,
  the Yamanouchi Foundation for Research on Metabolic Disorders, the Uehara Memorial
  Foundation, and the Inamori Foundation. The costs of publication of this article
  were defrayed in part by the payment of page charges. This article must therefore
  be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely
  to indicate this fact. \r\n\r\nWe are grateful to Akira Uesugi for photographic
  assistance."
article_processing_charge: No
article_type: original
author:
- first_name: Yoshiaki
  full_name: Nakajima, Yoshiaki
  last_name: Nakajima
- first_name: Hideki
  full_name: Iwakabe, Hideki
  last_name: Iwakabe
- first_name: Chihiro
  full_name: Akazawa, Chihiro
  last_name: Akazawa
- first_name: Hiroyuki
  full_name: Nawa, Hiroyuki
  last_name: Nawa
- first_name: Ryuichi
  full_name: Shigemoto, Ryuichi
  id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
  last_name: Shigemoto
  orcid: 0000-0001-8761-9444
- first_name: Noboru
  full_name: Mizuno, Noboru
  last_name: Mizuno
- first_name: Shigetada
  full_name: Nakanishi, Shigetada
  last_name: Nakanishi
citation:
  ama: Nakajima Y, Iwakabe H, Akazawa C, et al. Molecular characterization of a novel
    retinal metabotropic glutamate receptor mGluR6 with a high agonist selectivity
    for L-2-amino-4- phosphonobutyrate. <i>Journal of Biological Chemistry</i>. 1993;268(16):11868-11873.
    doi:<a href="https://doi.org/10.1016/S0021-9258(19)50280-0">10.1016/S0021-9258(19)50280-0</a>
  apa: Nakajima, Y., Iwakabe, H., Akazawa, C., Nawa, H., Shigemoto, R., Mizuno, N.,
    &#38; Nakanishi, S. (1993). Molecular characterization of a novel retinal metabotropic
    glutamate receptor mGluR6 with a high agonist selectivity for L-2-amino-4- phosphonobutyrate.
    <i>Journal of Biological Chemistry</i>. American Society for Biochemistry and
    Molecular Biology. <a href="https://doi.org/10.1016/S0021-9258(19)50280-0">https://doi.org/10.1016/S0021-9258(19)50280-0</a>
  chicago: Nakajima, Yoshiaki, Hideki Iwakabe, Chihiro Akazawa, Hiroyuki Nawa, Ryuichi
    Shigemoto, Noboru Mizuno, and Shigetada Nakanishi. “Molecular Characterization
    of a Novel Retinal Metabotropic Glutamate Receptor MGluR6 with a High Agonist
    Selectivity for L-2-Amino-4- Phosphonobutyrate.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry and Molecular Biology, 1993. <a href="https://doi.org/10.1016/S0021-9258(19)50280-0">https://doi.org/10.1016/S0021-9258(19)50280-0</a>.
  ieee: Y. Nakajima <i>et al.</i>, “Molecular characterization of a novel retinal
    metabotropic glutamate receptor mGluR6 with a high agonist selectivity for L-2-amino-4-
    phosphonobutyrate,” <i>Journal of Biological Chemistry</i>, vol. 268, no. 16.
    American Society for Biochemistry and Molecular Biology, pp. 11868–11873, 1993.
  ista: Nakajima Y, Iwakabe H, Akazawa C, Nawa H, Shigemoto R, Mizuno N, Nakanishi
    S. 1993. Molecular characterization of a novel retinal metabotropic glutamate
    receptor mGluR6 with a high agonist selectivity for L-2-amino-4- phosphonobutyrate.
    Journal of Biological Chemistry. 268(16), 11868–11873.
  mla: Nakajima, Yoshiaki, et al. “Molecular Characterization of a Novel Retinal Metabotropic
    Glutamate Receptor MGluR6 with a High Agonist Selectivity for L-2-Amino-4- Phosphonobutyrate.”
    <i>Journal of Biological Chemistry</i>, vol. 268, no. 16, American Society for
    Biochemistry and Molecular Biology, 1993, pp. 11868–73, doi:<a href="https://doi.org/10.1016/S0021-9258(19)50280-0">10.1016/S0021-9258(19)50280-0</a>.
  short: Y. Nakajima, H. Iwakabe, C. Akazawa, H. Nawa, R. Shigemoto, N. Mizuno, S.
    Nakanishi, Journal of Biological Chemistry 268 (1993) 11868–11873.
date_created: 2018-12-11T11:58:15Z
date_published: 1993-06-05T00:00:00Z
date_updated: 2022-04-26T06:56:15Z
day: '05'
doi: 10.1016/S0021-9258(19)50280-0
extern: '1'
external_id:
  pmid:
  - '8389366'
fulldoi: https://doi.org/10.1016/S0021-9258(19)50280-0
intvolume: '       268'
issue: '16'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1016/S0021-9258(19)50280-0
month: '06'
oa: 1
oa_version: Published Version
page: 11868 - 11873
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '4362'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Molecular characterization of a novel retinal metabotropic glutamate receptor
  mGluR6 with a high agonist selectivity for L-2-amino-4- phosphonobutyrate
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 268
year: '1993'
...
---
_id: '2539'
abstract:
- lang: eng
  text: cDNA clones for four different N-methyl-D-aspartate (NMDA) receptor subunits
    (NMDAR2A-NMDAR2D) were isolated through polymerase chain reactions followed by
    molecular screening of a rat brain cDNA library. These subunits are only about
    15% identical with the key subunit of the NMDA receptor (NMDAR1) but are highly
    homologous (~50% homology) with one another. They also commonly possess large
    hydrophilic domains at both amino- and carboxyl- terminal sides of the four putative
    transmembrane segments. NMDAR2A and NMDAR2C expressed individually in Xenopus
    oocytes showed no electrophysiological response to agonists. However, these subunits
    in combined expression with NMDAR1 markedly potentiated the NMDAR1 activity and
    produced functional variability in the affinity of agonists, the effectiveness
    of antagonists, and the sensitivity to Mg2+ blockade. Thus, NMDAR1 is essential
    for the function of the NMDA receptor, and multiple NMDAR2 subunits potentiate
    and differentiate the function of the NMDA receptor by forming different heteromeric
    configurations with NMDAR1. Northern blotting and in situ hybridization analyses
    revealed that the expressions of individual mRNAs for the NMDAR2 subunits overlap
    in some brain regions but are also specialized in many other regions. This investigation
    demonstrates the anatomical and functional differences of the NMDAR2 subunits,
    which provide the molecular basis for the functional diversity of the NMDA receptor.
acknowledgement: This work was supported in part by research grants from the Ministry
  of Education, Science, and Culture of Japan, the Ministry of Health and Welfare
  of Japan, the Senri Life Science Foundation, and Yamanouchi Foundation for Research
  on Metabolic Disorders. The costs of publication of this article were defrayed in
  part by the payment of page charges. This article must therefore be hereby marked
  “aduertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this
  fact.
article_processing_charge: No
article_type: original
author:
- first_name: Takahiro
  full_name: Ishii, Takahiro
  last_name: Ishii
- first_name: Koki
  full_name: Moriyoshi, Koki
  last_name: Moriyoshi
- first_name: Hidemitsu
  full_name: Sugihara, Hidemitsu
  last_name: Sugihara
- first_name: Kazuhir
  full_name: Sakurada, Kazuhir
  last_name: Sakurada
- first_name: Hiroshi
  full_name: Kadotani, Hiroshi
  last_name: Kadotani
- first_name: Mineto
  full_name: Yokoi, Mineto
  last_name: Yokoi
- first_name: Chihiro
  full_name: Akazawa, Chihiro
  last_name: Akazawa
- first_name: Ryuichi
  full_name: Shigemoto, Ryuichi
  id: 499F3ABC-F248-11E8-B48F-1D18A9856A87
  last_name: Shigemoto
  orcid: 0000-0001-8761-9444
- first_name: Noboru
  full_name: Mizuno, Noboru
  last_name: Mizuno
- first_name: Masayuki
  full_name: Masu, Masayuki
  last_name: Masu
- first_name: Shigetada
  full_name: Nakanishi, Shigetada
  last_name: Nakanishi
citation:
  ama: Ishii T, Moriyoshi K, Sugihara H, et al. Molecular characterization of the
    family of the N-methyl-D-aspartate receptor subunits. <i>Journal of Biological
    Chemistry</i>. 1993;268(4):2836-2843. doi:<a href="https://doi.org/10.1016/s0021-9258(18)53849-7
    ">10.1016/s0021-9258(18)53849-7 </a>
  apa: Ishii, T., Moriyoshi, K., Sugihara, H., Sakurada, K., Kadotani, H., Yokoi,
    M., … Nakanishi, S. (1993). Molecular characterization of the family of the N-methyl-D-aspartate
    receptor subunits. <i>Journal of Biological Chemistry</i>. American Society for
    Biochemistry and Molecular Biology. <a href="https://doi.org/10.1016/s0021-9258(18)53849-7
    ">https://doi.org/10.1016/s0021-9258(18)53849-7 </a>
  chicago: Ishii, Takahiro, Koki Moriyoshi, Hidemitsu Sugihara, Kazuhir Sakurada,
    Hiroshi Kadotani, Mineto Yokoi, Chihiro Akazawa, et al. “Molecular Characterization
    of the Family of the N-Methyl-D-Aspartate Receptor Subunits.” <i>Journal of Biological
    Chemistry</i>. American Society for Biochemistry and Molecular Biology, 1993.
    <a href="https://doi.org/10.1016/s0021-9258(18)53849-7 ">https://doi.org/10.1016/s0021-9258(18)53849-7
    </a>.
  ieee: T. Ishii <i>et al.</i>, “Molecular characterization of the family of the N-methyl-D-aspartate
    receptor subunits,” <i>Journal of Biological Chemistry</i>, vol. 268, no. 4. American
    Society for Biochemistry and Molecular Biology, pp. 2836–2843, 1993.
  ista: Ishii T, Moriyoshi K, Sugihara H, Sakurada K, Kadotani H, Yokoi M, Akazawa
    C, Shigemoto R, Mizuno N, Masu M, Nakanishi S. 1993. Molecular characterization
    of the family of the N-methyl-D-aspartate receptor subunits. Journal of Biological
    Chemistry. 268(4), 2836–2843.
  mla: Ishii, Takahiro, et al. “Molecular Characterization of the Family of the N-Methyl-D-Aspartate
    Receptor Subunits.” <i>Journal of Biological Chemistry</i>, vol. 268, no. 4, American
    Society for Biochemistry and Molecular Biology, 1993, pp. 2836–43, doi:<a href="https://doi.org/10.1016/s0021-9258(18)53849-7
    ">10.1016/s0021-9258(18)53849-7 </a>.
  short: T. Ishii, K. Moriyoshi, H. Sugihara, K. Sakurada, H. Kadotani, M. Yokoi,
    C. Akazawa, R. Shigemoto, N. Mizuno, M. Masu, S. Nakanishi, Journal of Biological
    Chemistry 268 (1993) 2836–2843.
date_created: 2018-12-11T11:58:16Z
date_published: 1993-02-05T00:00:00Z
date_updated: 2022-03-31T14:29:17Z
day: '05'
doi: '10.1016/s0021-9258(18)53849-7 '
extern: '1'
external_id:
  pmid:
  - '8428958'
fulldoi: 'https://doi.org/10.1016/s0021-9258(18)53849-7 '
intvolume: '       268'
issue: '4'
language:
- iso: eng
main_file_link:
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month: '02'
oa: 1
oa_version: Published Version
page: 2836 - 2843
pmid: 1
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
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publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '4360'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Molecular characterization of the family of the N-methyl-D-aspartate receptor
  subunits
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 268
year: '1993'
...