---
_id: '15146'
abstract:
- lang: eng
text: The extracellular matrix (ECM) serves as a scaffold for cells and plays an
essential role in regulating numerous cellular processes, including cell migration
and proliferation. Due to limitations in specimen preparation for conventional
room-temperature electron microscopy, we lack structural knowledge on how ECM
components are secreted, remodeled, and interact with surrounding cells. We have
developed a 3D-ECM platform compatible with sample thinning by cryo-focused ion
beam milling, the lift-out extraction procedure, and cryo-electron tomography.
Our workflow implements cell-derived matrices (CDMs) grown on EM grids, resulting
in a versatile tool closely mimicking ECM environments. This allows us to visualize
ECM for the first time in its hydrated, native context. Our data reveal an intricate
network of extracellular fibers, their positioning relative to matrix-secreting
cells, and previously unresolved structural entities. Our workflow and results
add to the structural atlas of the ECM, providing novel insights into its secretion
and assembly.
acknowledged_ssus:
- _id: LifeSc
- _id: ScienComp
- _id: EM-Fac
- _id: M-Shop
acknowledgement: "Open Access funding provided by IST Austria. We thank Armel Nicolas
and his team at the ISTA proteomics facility, Alois Schloegl, Stefano Elefante,
and colleagues at the ISTA Scientific Computing facility, Tommaso Constanzo and
Ludek Lovicar at the Electron Microsocpy Facility (EMF), and Thomas Menner at the
Miba Machine shop for their support. We also thank Wanda Kukulski (University of
Bern) as well as Darío Porley, Andreas Thader, and other members of the Schur group
for helpful discussions. Matt Swulius and Jessica Heebner provided great support
in using Dragonfly. We thank Dorotea Fracciolla (Art & Science) for support in figure
illustration.\r\n\r\nThis research was supported by the Scientific Service Units
of ISTA through resources provided by Scientific Computing, the Lab Support Facility,
and the Electron Microscopy Facility. We acknowledge funding support from the following
sources: Austrian Science Fund (FWF) grant P33367 (to F.K.M. Schur), the Federation
of European Biochemical Societies (to F.K.M. Schur), Niederösterreich (NÖ) Fonds
(to B. Zens), FWF grant E435 (to J.M. Hansen), European Research Council under the
European Union’s Horizon 2020 research (grant agreement No. 724373) (to M. Sixt),
and Jenny and Antti Wihuri Foundation (to J. Alanko). This publication has been
made possible in part by CZI grant DAF2021-234754 and grant DOI https://doi.org/10.37921/812628ebpcwg
from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community
Foundation (to F.K.M. Schur)."
article_number: e202309125
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Bettina
full_name: Zens, Bettina
id: 45FD126C-F248-11E8-B48F-1D18A9856A87
last_name: Zens
orcid: 0000-0002-9561-1239
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Jesse
full_name: Hansen, Jesse
id: 1063c618-6f9b-11ec-9123-f912fccded63
last_name: Hansen
orcid: 0000-0001-7967-2085
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
- first_name: Julia
full_name: Datler, Julia
id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
last_name: Datler
orcid: 0000-0002-3616-8580
- first_name: Victor-Valentin
full_name: Hodirnau, Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
orcid: 0000-0003-3904-947X
- first_name: Vanessa
full_name: Zheden, Vanessa
id: 39C5A68A-F248-11E8-B48F-1D18A9856A87
last_name: Zheden
orcid: 0000-0002-9438-4783
- first_name: Jonna H
full_name: Alanko, Jonna H
id: 2CC12E8C-F248-11E8-B48F-1D18A9856A87
last_name: Alanko
orcid: 0000-0002-7698-3061
- 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: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Zens B, Fäßler F, Hansen J, et al. Lift-out cryo-FIBSEM and cryo-ET reveal
the ultrastructural landscape of extracellular matrix. Journal of Cell Biology.
2024;223(6). doi:10.1083/jcb.202309125
apa: Zens, B., Fäßler, F., Hansen, J., Hauschild, R., Datler, J., Hodirnau, V.-V.,
… Schur, F. K. (2024). Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural
landscape of extracellular matrix. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.202309125
chicago: Zens, Bettina, Florian Fäßler, Jesse Hansen, Robert Hauschild, Julia Datler,
Victor-Valentin Hodirnau, Vanessa Zheden, Jonna H Alanko, Michael K Sixt, and
Florian KM Schur. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural
Landscape of Extracellular Matrix.” Journal of Cell Biology. Rockefeller
University Press, 2024. https://doi.org/10.1083/jcb.202309125.
ieee: B. Zens et al., “Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural
landscape of extracellular matrix,” Journal of Cell Biology, vol. 223,
no. 6. Rockefeller University Press, 2024.
ista: Zens B, Fäßler F, Hansen J, Hauschild R, Datler J, Hodirnau V-V, Zheden V,
Alanko JH, Sixt MK, Schur FK. 2024. Lift-out cryo-FIBSEM and cryo-ET reveal the
ultrastructural landscape of extracellular matrix. Journal of Cell Biology. 223(6),
e202309125.
mla: Zens, Bettina, et al. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural
Landscape of Extracellular Matrix.” Journal of Cell Biology, vol. 223,
no. 6, e202309125, Rockefeller University Press, 2024, doi:10.1083/jcb.202309125.
short: B. Zens, F. Fäßler, J. Hansen, R. Hauschild, J. Datler, V.-V. Hodirnau, V.
Zheden, J.H. Alanko, M.K. Sixt, F.K. Schur, Journal of Cell Biology 223 (2024).
corr_author: '1'
date_created: 2024-03-21T06:45:51Z
date_published: 2024-03-20T00:00:00Z
date_updated: 2025-09-04T13:17:16Z
day: '20'
ddc:
- '570'
department:
- _id: FlSc
- _id: MiSi
- _id: Bio
- _id: EM-Fac
doi: 10.1083/jcb.202309125
ec_funded: 1
external_id:
isi:
- '001264190100001'
pmid:
- '38506714'
file:
- access_level: open_access
checksum: 90d1984a93660735e506c2a304bc3f73
content_type: application/pdf
creator: dernst
date_created: 2024-03-25T12:52:04Z
date_updated: 2024-03-25T12:52:04Z
file_id: '15188'
file_name: 2024_JCB_Zens.pdf
file_size: 11907016
relation: main_file
success: 1
file_date_updated: 2024-03-25T12:52:04Z
has_accepted_license: '1'
intvolume: ' 223'
isi: 1
issue: '6'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
- _id: 7bd318a1-9f16-11ee-852c-cc9217763180
grant_number: E435
name: In Situ Actin Structures via Hybrid Cryo-electron Microscopy
- _id: 25FE9508-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '724373'
name: Cellular Navigation Along Spatial Gradients
- _id: 059B463C-7A3F-11EA-A408-12923DDC885E
name: "NÃ\x96-Fonds Preis für die Jungforscherin des Jahres am IST Austria"
- _id: 2615199A-B435-11E9-9278-68D0E5697425
grant_number: '21317'
name: Spatiotemporal regulation of chemokine-induced signalling in leukocyte chemotaxis
- _id: 62909c6f-2b32-11ec-9570-e1476aab5308
grant_number: CZI01
name: CryoMinflux-guided in-situ visual proteomics and structure determination
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular
matrix
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: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 223
year: '2024'
...
---
_id: '14788'
abstract:
- lang: eng
text: "Eukaryotic cells use clathrin-mediated endocytosis to take up a large range
of extracellular cargo. During endocytosis, a clathrin coat forms on the plasma
membrane, but it remains controversial when and how it is remodeled into a spherical
vesicle.\r\nHere, we use 3D superresolution microscopy to determine the precise
geometry of the clathrin coat at large numbers of endocytic sites. Through pseudo-temporal
sorting, we determine the average trajectory of clathrin remodeling during endocytosis.
We find that clathrin coats assemble first on flat membranes to 50% of the coat
area before they become rapidly and continuously bent, and this mechanism is confirmed
in three cell lines. We introduce the cooperative curvature model, which is based
on positive feedback for curvature generation. It accurately describes the measured
shapes and dynamics of the clathrin coat and could represent a general mechanism
for clathrin coat remodeling on the plasma membrane."
acknowledgement: We thank the entire Ries and Kaksonen labs for fruitful discussions
and support. This work was supported by the European Research Council (ERC CoG-724489
to J. Ries), the National Institutes of Health Common Fund 4D Nucleome Program (Grant
U01 to J. Ries), the Human Frontier Science Program (RGY0065/2017 to J. Ries), the
EMBL Interdisciplinary Postdoc Programme (EIPOD) under Marie Curie Actions COFUND
(Grant 229597 to O. Avinoam), the European Molecular Biology Laboratory (M. Mund,
A. Tschanz, Y.-L. Wu and J. Ries), and the Swiss National Science Foundation (grant
310030B_182825 and NCCR Chemical Biology to M. Kaksonen). O. Avinoam is an incumbent
of the Miriam Berman Presidential Development Chair.
article_number: e202206038
article_processing_charge: No
article_type: original
author:
- first_name: Markus
full_name: Mund, Markus
last_name: Mund
- first_name: Aline
full_name: Tschanz, Aline
last_name: Tschanz
- first_name: Yu-Le
full_name: Wu, Yu-Le
last_name: Wu
- first_name: Felix F
full_name: Frey, Felix F
id: a0270b37-8f1a-11ec-95c7-8e710c59a4f3
last_name: Frey
orcid: 0000-0001-8501-6017
- first_name: Johanna L.
full_name: Mehl, Johanna L.
last_name: Mehl
- first_name: Marko
full_name: Kaksonen, Marko
last_name: Kaksonen
- first_name: Ori
full_name: Avinoam, Ori
last_name: Avinoam
- first_name: Ulrich S.
full_name: Schwarz, Ulrich S.
last_name: Schwarz
- first_name: Jonas
full_name: Ries, Jonas
last_name: Ries
citation:
ama: Mund M, Tschanz A, Wu Y-L, et al. Clathrin coats partially preassemble and
subsequently bend during endocytosis. Journal of Cell Biology. 2023;222(3).
doi:10.1083/jcb.202206038
apa: Mund, M., Tschanz, A., Wu, Y.-L., Frey, F. F., Mehl, J. L., Kaksonen, M., …
Ries, J. (2023). Clathrin coats partially preassemble and subsequently bend during
endocytosis. Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.202206038
chicago: Mund, Markus, Aline Tschanz, Yu-Le Wu, Felix F Frey, Johanna L. Mehl, Marko
Kaksonen, Ori Avinoam, Ulrich S. Schwarz, and Jonas Ries. “Clathrin Coats Partially
Preassemble and Subsequently Bend during Endocytosis.” Journal of Cell Biology.
Rockefeller University Press, 2023. https://doi.org/10.1083/jcb.202206038.
ieee: M. Mund et al., “Clathrin coats partially preassemble and subsequently
bend during endocytosis,” Journal of Cell Biology, vol. 222, no. 3. Rockefeller
University Press, 2023.
ista: Mund M, Tschanz A, Wu Y-L, Frey FF, Mehl JL, Kaksonen M, Avinoam O, Schwarz
US, Ries J. 2023. Clathrin coats partially preassemble and subsequently bend during
endocytosis. Journal of Cell Biology. 222(3), e202206038.
mla: Mund, Markus, et al. “Clathrin Coats Partially Preassemble and Subsequently
Bend during Endocytosis.” Journal of Cell Biology, vol. 222, no. 3, e202206038,
Rockefeller University Press, 2023, doi:10.1083/jcb.202206038.
short: M. Mund, A. Tschanz, Y.-L. Wu, F.F. Frey, J.L. Mehl, M. Kaksonen, O. Avinoam,
U.S. Schwarz, J. Ries, Journal of Cell Biology 222 (2023).
date_created: 2024-01-10T10:45:55Z
date_published: 2023-02-03T00:00:00Z
date_updated: 2024-01-16T10:17:05Z
day: '03'
ddc:
- '570'
department:
- _id: AnSa
doi: 10.1083/jcb.202206038
external_id:
isi:
- '000978065000001'
pmid:
- '36734980'
file:
- access_level: open_access
checksum: 505d5cac36c14b073b68c7fed1a92bd3
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T10:15:09Z
date_updated: 2024-01-16T10:15:09Z
file_id: '14811'
file_name: 2023_JCB_Mund.pdf
file_size: 5678069
relation: main_file
success: 1
file_date_updated: 2024-01-16T10:15:09Z
has_accepted_license: '1'
intvolume: ' 222'
isi: 1
issue: '3'
keyword:
- Cell Biology
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
status: public
title: Clathrin coats partially preassemble and subsequently bend during endocytosis
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: 222
year: '2023'
...
---
_id: '12121'
abstract:
- lang: eng
text: Autophagosomes are double-membraned vesicles that traffic harmful or unwanted
cellular macromolecules to the vacuole for recycling. Although autophagosome biogenesis
has been extensively studied, autophagosome maturation, i.e., delivery and fusion
with the vacuole, remains largely unknown in plants. Here, we have identified
an autophagy adaptor, CFS1, that directly interacts with the autophagosome marker
ATG8 and localizes on both membranes of the autophagosome. Autophagosomes form
normally in Arabidopsis thaliana cfs1 mutants, but their delivery to the vacuole
is disrupted. CFS1’s function is evolutionarily conserved in plants, as it also
localizes to the autophagosomes and plays a role in autophagic flux in the liverwort
Marchantia polymorpha. CFS1 regulates autophagic flux by bridging autophagosomes
with the multivesicular body-localized ESCRT-I component VPS23A, leading to the
formation of amphisomes. Similar to CFS1-ATG8 interaction, disrupting the CFS1-VPS23A
interaction blocks autophagic flux and renders plants sensitive to nitrogen starvation.
Altogether, our results reveal a conserved vacuolar sorting hub that regulates
autophagic flux in plants.
acknowledgement: "We thank Suayip Ustün, Karin Schumacher, Erika Isono, Gerd Juergens,
Takashi Ueda, Daniel Hofius, and Liwen Jiang for sharing published materials.\r\nWe
acknowledge funding from Austrian Academy of Sciences, Austrian Science Fund (FWF,
P 32355, P 34944), Austrian Science Fund (FWF-SFB F79), Vienna Science and Technology\r\nFund
(WWTF, LS17-047) to Y. Dagdas; Austrian Academy of Sciences DOC Fellowship to J.
Zhao, Marie Curie VIP2 Fellowship to J.C. De La Concepcion and M. Clavel; Hong Kong
Research Grant Council (GRF14121019, 14113921, AoE/M-05/12, C4002-17G) to B.-H.
Kang. We thank Vienna Biocenter Core Facilities (VBCF) Protein Chemistry, Biooptics,
Plant Sciences, Molecular Biology, and Protein Technologies. We thank J. Matthew
Watson\r\nand members of the Dagdas lab for the critical reading and editing of
the manuscript."
article_number: e202203139
article_processing_charge: No
article_type: original
author:
- first_name: Jierui
full_name: Zhao, Jierui
last_name: Zhao
- first_name: Mai Thu
full_name: Bui, Mai Thu
last_name: Bui
- first_name: Juncai
full_name: Ma, Juncai
last_name: Ma
- first_name: Fabian
full_name: Künzl, Fabian
last_name: Künzl
- first_name: Lorenzo
full_name: Picchianti, Lorenzo
last_name: Picchianti
- first_name: Juan Carlos
full_name: De La Concepcion, Juan Carlos
last_name: De La Concepcion
- first_name: Yixuan
full_name: Chen, Yixuan
last_name: Chen
- first_name: Sofia
full_name: Petsangouraki, Sofia
last_name: Petsangouraki
- first_name: Azadeh
full_name: Mohseni, Azadeh
last_name: Mohseni
- first_name: Marta
full_name: García-Leon, Marta
last_name: García-Leon
- first_name: Marta Salas
full_name: Gomez, Marta Salas
last_name: Gomez
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
- first_name: Dubois
full_name: Gwennogan, Dubois
last_name: Gwennogan
- first_name: Roksolana
full_name: Kobylinska, Roksolana
last_name: Kobylinska
- first_name: Marion
full_name: Clavel, Marion
last_name: Clavel
- first_name: Swen
full_name: Schellmann, Swen
last_name: Schellmann
- first_name: Yvon
full_name: Jaillais, Yvon
last_name: Jaillais
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Byung-Ho
full_name: Kang, Byung-Ho
last_name: Kang
- first_name: Yasin
full_name: Dagdas, Yasin
last_name: Dagdas
citation:
ama: Zhao J, Bui MT, Ma J, et al. Plant autophagosomes mature into amphisomes prior
to their delivery to the central vacuole. Journal of Cell Biology. 2022;221(12).
doi:10.1083/jcb.202203139
apa: Zhao, J., Bui, M. T., Ma, J., Künzl, F., Picchianti, L., De La Concepcion,
J. C., … Dagdas, Y. (2022). Plant autophagosomes mature into amphisomes prior
to their delivery to the central vacuole. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.202203139
chicago: Zhao, Jierui, Mai Thu Bui, Juncai Ma, Fabian Künzl, Lorenzo Picchianti,
Juan Carlos De La Concepcion, Yixuan Chen, et al. “Plant Autophagosomes Mature
into Amphisomes Prior to Their Delivery to the Central Vacuole.” Journal of
Cell Biology. Rockefeller University Press, 2022. https://doi.org/10.1083/jcb.202203139.
ieee: J. Zhao et al., “Plant autophagosomes mature into amphisomes prior
to their delivery to the central vacuole,” Journal of Cell Biology, vol.
221, no. 12. Rockefeller University Press, 2022.
ista: Zhao J, Bui MT, Ma J, Künzl F, Picchianti L, De La Concepcion JC, Chen Y,
Petsangouraki S, Mohseni A, García-Leon M, Gomez MS, Giannini C, Gwennogan D,
Kobylinska R, Clavel M, Schellmann S, Jaillais Y, Friml J, Kang B-H, Dagdas Y.
2022. Plant autophagosomes mature into amphisomes prior to their delivery to the
central vacuole. Journal of Cell Biology. 221(12), e202203139.
mla: Zhao, Jierui, et al. “Plant Autophagosomes Mature into Amphisomes Prior to
Their Delivery to the Central Vacuole.” Journal of Cell Biology, vol. 221,
no. 12, e202203139, Rockefeller University Press, 2022, doi:10.1083/jcb.202203139.
short: J. Zhao, M.T. Bui, J. Ma, F. Künzl, L. Picchianti, J.C. De La Concepcion,
Y. Chen, S. Petsangouraki, A. Mohseni, M. García-Leon, M.S. Gomez, C. Giannini,
D. Gwennogan, R. Kobylinska, M. Clavel, S. Schellmann, Y. Jaillais, J. Friml,
B.-H. Kang, Y. Dagdas, Journal of Cell Biology 221 (2022).
date_created: 2023-01-12T11:57:10Z
date_published: 2022-12-01T00:00:00Z
date_updated: 2023-08-03T14:20:15Z
day: '01'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1083/jcb.202203139
external_id:
isi:
- '000932958800001'
pmid:
- '36260289'
file:
- access_level: open_access
checksum: 050b5cc4b25e6b94fe3e3cbfe0f5c06b
content_type: application/pdf
creator: dernst
date_created: 2023-01-23T10:30:11Z
date_updated: 2023-01-23T10:30:11Z
file_id: '12342'
file_name: 2022_JCB_Zhao.pdf
file_size: 10365777
relation: main_file
success: 1
file_date_updated: 2023-01-23T10:30:11Z
has_accepted_license: '1'
intvolume: ' 221'
isi: 1
issue: '12'
keyword:
- Cell Biology
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Plant autophagosomes mature into amphisomes prior to their delivery to the
central vacuole
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: 221
year: '2022'
...
---
_id: '12122'
abstract:
- lang: eng
text: Centrosomes play a crucial role during immune cell interactions and initiation
of the immune response. In proliferating cells, centrosome numbers are tightly
controlled and generally limited to one in G1 and two prior to mitosis. Defects
in regulating centrosome numbers have been associated with cell transformation
and tumorigenesis. Here, we report the emergence of extra centrosomes in leukocytes
during immune activation. Upon antigen encounter, dendritic cells pass through
incomplete mitosis and arrest in the subsequent G1 phase leading to tetraploid
cells with accumulated centrosomes. In addition, cell stimulation increases expression
of polo-like kinase 2, resulting in diploid cells with two centrosomes in G1-arrested
cells. During cell migration, centrosomes tightly cluster and act as functional
microtubule-organizing centers allowing for increased persistent locomotion along
gradients of chemotactic cues. Moreover, dendritic cells with extra centrosomes
display enhanced secretion of inflammatory cytokines and optimized T cell responses.
Together, these results demonstrate a previously unappreciated role of extra centrosomes
for regular cell and tissue homeostasis.
acknowledgement: "We thank Markéta Dalecká and Irena Krejzová for their support with
FIB-SEM imaging, the Imaging Methods Core Facility at BIOCEV supported by the Ministry
of Education, Youth and Sports Czech Republic (Large RI Project LM2018129 Czech-BioImaging),
and European Regional Development Fund (project No. CZ.02.1.01/0.0/0.0/18_046/0016045)
for their support with obtaining imaging data presented in this paper. The authors
further thank Andreas Villunger, Florian Gärtner, Frank Bradke, and Sarah Förster
for helpful discussions; Andy Zielinski for help with statistics; and Björn Weiershausen
for assisting with figure illustration.\r\n\r\nThis work was funded by a fellowship
of the Ministry of Innovation, Science and Research of North-Rhine-Westphalia (AZ:
421-8.03.03.02-137069) to E. Kiermaier and the Deutsche Forschungsgemeinschaft (German
Research Foundation) under Germany’s Excellence Strategy – EXC 2151 – 390873048.
R. Hauschild was funded by grant number 2020-225401 from the Chan Zuckerberg Initiative
Donor-Advised Fund, an advised fund of Silicon Valley Community Foundation. M. Hons
is supported by Czech Science Foundation GACR 20-24603Y and Charles University PRIMUS/20/MED/013."
article_number: e202107134
article_processing_charge: No
article_type: original
author:
- first_name: Ann-Kathrin
full_name: Weier, Ann-Kathrin
last_name: Weier
- first_name: Mirka
full_name: Homrich, Mirka
last_name: Homrich
- first_name: Stephanie
full_name: Ebbinghaus, Stephanie
last_name: Ebbinghaus
- first_name: Pavel
full_name: Juda, Pavel
last_name: Juda
- first_name: Eliška
full_name: Miková, Eliška
last_name: Miková
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
- first_name: Lili
full_name: Zhang, Lili
last_name: Zhang
- first_name: Thomas
full_name: Quast, Thomas
last_name: Quast
- first_name: Elvira
full_name: Mass, Elvira
last_name: Mass
- first_name: Andreas
full_name: Schlitzer, Andreas
last_name: Schlitzer
- first_name: Waldemar
full_name: Kolanus, Waldemar
last_name: Kolanus
- first_name: Sven
full_name: Burgdorf, Sven
last_name: Burgdorf
- first_name: Oliver J.
full_name: Gruß, Oliver J.
last_name: Gruß
- first_name: Miroslav
full_name: Hons, Miroslav
last_name: Hons
- first_name: Stefan
full_name: Wieser, Stefan
last_name: Wieser
- first_name: Eva
full_name: Kiermaier, Eva
last_name: Kiermaier
citation:
ama: Weier A-K, Homrich M, Ebbinghaus S, et al. Multiple centrosomes enhance migration
and immune cell effector functions of mature dendritic cells. Journal of Cell
Biology. 2022;221(12). doi:10.1083/jcb.202107134
apa: Weier, A.-K., Homrich, M., Ebbinghaus, S., Juda, P., Miková, E., Hauschild,
R., … Kiermaier, E. (2022). Multiple centrosomes enhance migration and immune
cell effector functions of mature dendritic cells. Journal of Cell Biology.
Rockefeller University Press. https://doi.org/10.1083/jcb.202107134
chicago: Weier, Ann-Kathrin, Mirka Homrich, Stephanie Ebbinghaus, Pavel Juda, Eliška
Miková, Robert Hauschild, Lili Zhang, et al. “Multiple Centrosomes Enhance Migration
and Immune Cell Effector Functions of Mature Dendritic Cells.” Journal of Cell
Biology. Rockefeller University Press, 2022. https://doi.org/10.1083/jcb.202107134.
ieee: A.-K. Weier et al., “Multiple centrosomes enhance migration and immune
cell effector functions of mature dendritic cells,” Journal of Cell Biology,
vol. 221, no. 12. Rockefeller University Press, 2022.
ista: Weier A-K, Homrich M, Ebbinghaus S, Juda P, Miková E, Hauschild R, Zhang L,
Quast T, Mass E, Schlitzer A, Kolanus W, Burgdorf S, Gruß OJ, Hons M, Wieser S,
Kiermaier E. 2022. Multiple centrosomes enhance migration and immune cell effector
functions of mature dendritic cells. Journal of Cell Biology. 221(12), e202107134.
mla: Weier, Ann-Kathrin, et al. “Multiple Centrosomes Enhance Migration and Immune
Cell Effector Functions of Mature Dendritic Cells.” Journal of Cell Biology,
vol. 221, no. 12, e202107134, Rockefeller University Press, 2022, doi:10.1083/jcb.202107134.
short: A.-K. Weier, M. Homrich, S. Ebbinghaus, P. Juda, E. Miková, R. Hauschild,
L. Zhang, T. Quast, E. Mass, A. Schlitzer, W. Kolanus, S. Burgdorf, O.J. Gruß,
M. Hons, S. Wieser, E. Kiermaier, Journal of Cell Biology 221 (2022).
date_created: 2023-01-12T12:01:09Z
date_published: 2022-12-05T00:00:00Z
date_updated: 2025-04-15T08:37:41Z
day: '05'
ddc:
- '570'
department:
- _id: Bio
doi: 10.1083/jcb.202107134
external_id:
isi:
- '000932941400001'
pmid:
- '36214847 '
file:
- access_level: open_access
checksum: 0c9af38f82af30c6ce528f2caece4246
content_type: application/pdf
creator: dernst
date_created: 2023-08-16T11:24:53Z
date_updated: 2023-08-16T11:24:53Z
file_id: '14065'
file_name: 2023_JCB_Weier.pdf
file_size: 11090179
relation: main_file
success: 1
file_date_updated: 2023-08-16T11:24:53Z
has_accepted_license: '1'
intvolume: ' 221'
isi: 1
issue: '12'
keyword:
- Cell Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-sa/4.0/
month: '12'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: c08e9ad1-5a5b-11eb-8a69-9d1cf3b07473
grant_number: CZI01
name: Tools for automation and feedback microscopy
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Multiple centrosomes enhance migration and immune cell effector functions of
mature dendritic cells
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 221
year: '2022'
...
---
_id: '12080'
abstract:
- lang: eng
text: 'Endocytosis is a multistep process involving the sequential recruitment and
action of numerous proteins. This process can be divided into two phases: an early
phase, in which sites of endocytosis are formed, and a late phase in which clathrin-coated
vesicles are formed and internalized into the cytosol, but how these phases link
to each other remains unclear. In this study, we demonstrate that anchoring the
yeast Eps15-like protein Pan1p to the peroxisome triggers most of the events occurring
during the late phase at the peroxisome. At this ectopic location, Pan1p recruits
most proteins that function in the late phases—including actin nucleation promoting
factors—and then initiates actin polymerization. Pan1p also recruited Prk1 kinase
and actin depolymerizing factors, thereby triggering disassembly immediately after
actin assembly and inducing dissociation of endocytic proteins from the peroxisome.
These observations suggest that Pan1p is a key regulator for initiating, processing,
and completing the late phase of endocytosis.'
acknowledgement: 'This work was supported by JSPS KAKENHI GRANT #18K062291, and the
Takeda Science Foundation to J.Y. Toshima, as well as JSPS KAKENHI GRANT #19K065710,
the Uehara Memorial Foundation, and Life Science Foundation of JAPAN to J. Toshima.'
article_number: e202112138
article_processing_charge: No
article_type: original
author:
- first_name: Mariko
full_name: Enshoji, Mariko
last_name: Enshoji
- first_name: Yoshiko
full_name: Miyano, Yoshiko
last_name: Miyano
- first_name: Nao
full_name: Yoshida, Nao
last_name: Yoshida
- first_name: Makoto
full_name: Nagano, Makoto
last_name: Nagano
- first_name: Minami
full_name: Watanabe, Minami
last_name: Watanabe
- first_name: Mayumi
full_name: Kunihiro, Mayumi
last_name: Kunihiro
- 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: Junko Y.
full_name: Toshima, Junko Y.
last_name: Toshima
- first_name: Jiro
full_name: Toshima, Jiro
last_name: Toshima
citation:
ama: Enshoji M, Miyano Y, Yoshida N, et al. Eps15/Pan1p is a master regulator of
the late stages of the endocytic pathway. Journal of Cell Biology. 2022;221(10).
doi:10.1083/jcb.202112138
apa: Enshoji, M., Miyano, Y., Yoshida, N., Nagano, M., Watanabe, M., Kunihiro, M.,
… Toshima, J. (2022). Eps15/Pan1p is a master regulator of the late stages of
the endocytic pathway. Journal of Cell Biology. Rockefeller University
Press. https://doi.org/10.1083/jcb.202112138
chicago: Enshoji, Mariko, Yoshiko Miyano, Nao Yoshida, Makoto Nagano, Minami Watanabe,
Mayumi Kunihiro, Daria E Siekhaus, Junko Y. Toshima, and Jiro Toshima. “Eps15/Pan1p
Is a Master Regulator of the Late Stages of the Endocytic Pathway.” Journal
of Cell Biology. Rockefeller University Press, 2022. https://doi.org/10.1083/jcb.202112138.
ieee: M. Enshoji et al., “Eps15/Pan1p is a master regulator of the late stages
of the endocytic pathway,” Journal of Cell Biology, vol. 221, no. 10. Rockefeller
University Press, 2022.
ista: Enshoji M, Miyano Y, Yoshida N, Nagano M, Watanabe M, Kunihiro M, Siekhaus
DE, Toshima JY, Toshima J. 2022. Eps15/Pan1p is a master regulator of the late
stages of the endocytic pathway. Journal of Cell Biology. 221(10), e202112138.
mla: Enshoji, Mariko, et al. “Eps15/Pan1p Is a Master Regulator of the Late Stages
of the Endocytic Pathway.” Journal of Cell Biology, vol. 221, no. 10, e202112138,
Rockefeller University Press, 2022, doi:10.1083/jcb.202112138.
short: M. Enshoji, Y. Miyano, N. Yoshida, M. Nagano, M. Watanabe, M. Kunihiro, D.E.
Siekhaus, J.Y. Toshima, J. Toshima, Journal of Cell Biology 221 (2022).
date_created: 2022-09-11T22:01:54Z
date_published: 2022-08-19T00:00:00Z
date_updated: 2023-08-03T13:49:07Z
day: '19'
ddc:
- '570'
department:
- _id: DaSi
doi: 10.1083/jcb.202112138
external_id:
isi:
- '000932770500001'
pmid:
- '35984332'
file:
- access_level: open_access
checksum: f2e581e66b5cdab9df81b56e850b3eaa
content_type: application/pdf
creator: dernst
date_created: 2023-01-20T09:32:53Z
date_updated: 2023-02-21T23:30:39Z
embargo: 2023-02-20
file_id: '12321'
file_name: 2022_JCB_Enshoji.pdf
file_size: 7816875
relation: main_file
file_date_updated: 2023-02-21T23:30:39Z
has_accepted_license: '1'
intvolume: ' 221'
isi: 1
issue: '10'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Eps15/Pan1p is a master regulator of the late stages of the endocytic pathway
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 221
year: '2022'
...
---
_id: '12272'
abstract:
- lang: eng
text: Reading, interpreting and crawling along gradients of chemotactic cues is
one of the most complex questions in cell biology. In this issue, Georgantzoglou
et al. (2022. J. Cell. Biol.https://doi.org/10.1083/jcb.202103207) use in vivo
models to map the temporal sequence of how neutrophils respond to an acutely arising
gradient of chemoattractant.
article_number: e202206127
article_processing_charge: No
article_type: original
author:
- first_name: Julian A
full_name: Stopp, Julian A
id: 489E3F00-F248-11E8-B48F-1D18A9856A87
last_name: Stopp
- first_name: Michael K
full_name: Sixt, Michael K
id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
last_name: Sixt
orcid: 0000-0002-6620-9179
citation:
ama: 'Stopp JA, Sixt MK. Plan your trip before you leave: The neutrophils’ search-and-run
journey. Journal of Cell Biology. 2022;221(8). doi:10.1083/jcb.202206127'
apa: 'Stopp, J. A., & Sixt, M. K. (2022). Plan your trip before you leave: The
neutrophils’ search-and-run journey. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.202206127'
chicago: 'Stopp, Julian A, and Michael K Sixt. “Plan Your Trip before You Leave:
The Neutrophils’ Search-and-Run Journey.” Journal of Cell Biology. Rockefeller
University Press, 2022. https://doi.org/10.1083/jcb.202206127.'
ieee: 'J. A. Stopp and M. K. Sixt, “Plan your trip before you leave: The neutrophils’
search-and-run journey,” Journal of Cell Biology, vol. 221, no. 8. Rockefeller
University Press, 2022.'
ista: 'Stopp JA, Sixt MK. 2022. Plan your trip before you leave: The neutrophils’
search-and-run journey. Journal of Cell Biology. 221(8), e202206127.'
mla: 'Stopp, Julian A., and Michael K. Sixt. “Plan Your Trip before You Leave: The
Neutrophils’ Search-and-Run Journey.” Journal of Cell Biology, vol. 221,
no. 8, e202206127, Rockefeller University Press, 2022, doi:10.1083/jcb.202206127.'
short: J.A. Stopp, M.K. Sixt, Journal of Cell Biology 221 (2022).
corr_author: '1'
date_created: 2023-01-16T10:01:08Z
date_published: 2022-07-20T00:00:00Z
date_updated: 2026-04-26T22:30:26Z
day: '20'
ddc:
- '570'
department:
- _id: MiSi
doi: 10.1083/jcb.202206127
external_id:
isi:
- '000874717200001'
pmid:
- '35856919'
file:
- access_level: open_access
checksum: 6b1620743669679b48b9389bb40f5a11
content_type: application/pdf
creator: dernst
date_created: 2023-01-30T10:39:34Z
date_updated: 2023-01-30T10:39:34Z
file_id: '12451'
file_name: 2022_JourCellBiology_Stopp.pdf
file_size: 969969
relation: main_file
success: 1
file_date_updated: 2023-01-30T10:39:34Z
has_accepted_license: '1'
intvolume: ' 221'
isi: 1
issue: '8'
keyword:
- Cell Biology
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
related_material:
record:
- id: '14697'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: 'Plan your trip before you leave: The neutrophils’ search-and-run journey'
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 221
year: '2022'
...
---
_id: '10337'
abstract:
- lang: eng
text: The T cell receptor (TCR) pathway receives, processes, and amplifies the signal
from pathogenic antigens to the activation of T cells. Although major components
in this pathway have been identified, the knowledge on how individual components
cooperate to effectively transduce signals remains limited. Phase separation emerges
as a biophysical principle in organizing signaling molecules into liquid-like
condensates. Here, we report that phospholipase Cγ1 (PLCγ1) promotes phase separation
of LAT, a key adaptor protein in the TCR pathway. PLCγ1 directly cross-links LAT
through its two SH2 domains. PLCγ1 also protects LAT from dephosphorylation by
the phosphatase CD45 and promotes LAT-dependent ERK activation and SLP76 phosphorylation.
Intriguingly, a nonmonotonic effect of PLCγ1 on LAT clustering was discovered.
Computer simulations, based on patchy particles, revealed how the cluster size
is regulated by protein compositions. Together, these results define a critical
function of PLCγ1 in promoting phase separation of the LAT complex and TCR signal
transduction.
acknowledgement: Charles H. Hood Foundation (NO AWARD) ; Rally Foundation (NO AWARD)
article_number: e202009154
article_processing_charge: No
article_type: original
author:
- first_name: Longhui
full_name: Zeng, Longhui
last_name: Zeng
- first_name: Ivan
full_name: Palaia, Ivan
last_name: Palaia
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Xiaolei
full_name: Su, Xiaolei
last_name: Su
citation:
ama: Zeng L, Palaia I, Šarić A, Su X. PLCγ1 promotes phase separation of T cell
signaling components. Journal of Cell Biology. 2021;220(6). doi:10.1083/jcb.202009154
apa: Zeng, L., Palaia, I., Šarić, A., & Su, X. (2021). PLCγ1 promotes phase
separation of T cell signaling components. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.202009154
chicago: Zeng, Longhui, Ivan Palaia, Anđela Šarić, and Xiaolei Su. “PLCγ1 Promotes
Phase Separation of T Cell Signaling Components.” Journal of Cell Biology.
Rockefeller University Press, 2021. https://doi.org/10.1083/jcb.202009154.
ieee: L. Zeng, I. Palaia, A. Šarić, and X. Su, “PLCγ1 promotes phase separation
of T cell signaling components,” Journal of Cell Biology, vol. 220, no.
6. Rockefeller University Press, 2021.
ista: Zeng L, Palaia I, Šarić A, Su X. 2021. PLCγ1 promotes phase separation of
T cell signaling components. Journal of Cell Biology. 220(6), e202009154.
mla: Zeng, Longhui, et al. “PLCγ1 Promotes Phase Separation of T Cell Signaling
Components.” Journal of Cell Biology, vol. 220, no. 6, e202009154, Rockefeller
University Press, 2021, doi:10.1083/jcb.202009154.
short: L. Zeng, I. Palaia, A. Šarić, X. Su, Journal of Cell Biology 220 (2021).
date_created: 2021-11-25T15:21:30Z
date_published: 2021-04-30T00:00:00Z
date_updated: 2021-11-25T15:33:08Z
day: '30'
doi: 10.1083/jcb.202009154
extern: '1'
external_id:
pmid:
- '33929486'
intvolume: ' 220'
issue: '6'
keyword:
- cell biology
language:
- iso: eng
month: '04'
oa_version: None
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: PLCγ1 promotes phase separation of T cell signaling components
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 220
year: '2021'
...
---
_id: '9094'
abstract:
- lang: eng
text: Dendritic cells (DCs) are crucial for the priming of naive T cells and the
initiation of adaptive immunity. Priming is initiated at a heterologous cell–cell
contact, the immunological synapse (IS). While it is established that F-actin
dynamics regulates signaling at the T cell side of the contact, little is known
about the cytoskeletal contribution on the DC side. Here, we show that the DC
actin cytoskeleton is decisive for the formation of a multifocal synaptic structure,
which correlates with T cell priming efficiency. DC actin at the IS appears in
transient foci that are dynamized by the WAVE regulatory complex (WRC). The absence
of the WRC in DCs leads to stabilized contacts with T cells, caused by an increase
in ICAM1-integrin–mediated cell–cell adhesion. This results in lower numbers of
activated and proliferating T cells, demonstrating an important role for DC actin
in the regulation of immune synapse functionality.
article_number: e202006081
article_processing_charge: No
article_type: original
author:
- first_name: Alexander F
full_name: Leithner, Alexander F
id: 3B1B77E4-F248-11E8-B48F-1D18A9856A87
last_name: Leithner
orcid: 0000-0002-1073-744X
- first_name: LM
full_name: Altenburger, LM
last_name: Altenburger
- first_name: R
full_name: Hauschild, R
last_name: Hauschild
- first_name: Frank P
full_name: Assen, Frank P
id: 3A8E7F24-F248-11E8-B48F-1D18A9856A87
last_name: Assen
orcid: 0000-0003-3470-6119
- first_name: K
full_name: Rottner, K
last_name: Rottner
- first_name: Stradal
full_name: TEB, Stradal
last_name: TEB
- first_name: A
full_name: Diz-Muñoz, A
last_name: Diz-Muñoz
- first_name: JV
full_name: Stein, JV
last_name: Stein
- first_name: Michael K
full_name: Sixt, Michael K
id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
last_name: Sixt
orcid: 0000-0002-6620-9179
citation:
ama: Leithner AF, Altenburger L, Hauschild R, et al. Dendritic cell actin dynamics
control contact duration and priming efficiency at the immunological synapse.
Journal of Cell Biology. 2021;220(4). doi:10.1083/jcb.202006081
apa: Leithner, A. F., Altenburger, L., Hauschild, R., Assen, F. P., Rottner, K.,
TEB, S., … Sixt, M. K. (2021). Dendritic cell actin dynamics control contact duration
and priming efficiency at the immunological synapse. Journal of Cell Biology.
Rockefeller University Press. https://doi.org/10.1083/jcb.202006081
chicago: Leithner, Alexander F, LM Altenburger, R Hauschild, Frank P Assen, K Rottner,
Stradal TEB, A Diz-Muñoz, JV Stein, and Michael K Sixt. “Dendritic Cell Actin
Dynamics Control Contact Duration and Priming Efficiency at the Immunological
Synapse.” Journal of Cell Biology. Rockefeller University Press, 2021.
https://doi.org/10.1083/jcb.202006081.
ieee: A. F. Leithner et al., “Dendritic cell actin dynamics control contact
duration and priming efficiency at the immunological synapse,” Journal of Cell
Biology, vol. 220, no. 4. Rockefeller University Press, 2021.
ista: Leithner AF, Altenburger L, Hauschild R, Assen FP, Rottner K, TEB S, Diz-Muñoz
A, Stein J, Sixt MK. 2021. Dendritic cell actin dynamics control contact duration
and priming efficiency at the immunological synapse. Journal of Cell Biology.
220(4), e202006081.
mla: Leithner, Alexander F., et al. “Dendritic Cell Actin Dynamics Control Contact
Duration and Priming Efficiency at the Immunological Synapse.” Journal of Cell
Biology, vol. 220, no. 4, e202006081, Rockefeller University Press, 2021,
doi:10.1083/jcb.202006081.
short: A.F. Leithner, L. Altenburger, R. Hauschild, F.P. Assen, K. Rottner, S. TEB,
A. Diz-Muñoz, J. Stein, M.K. Sixt, Journal of Cell Biology 220 (2021).
corr_author: '1'
date_created: 2021-02-05T10:08:04Z
date_published: 2021-04-05T00:00:00Z
date_updated: 2024-10-09T21:00:23Z
day: '05'
ddc:
- '570'
department:
- _id: MiSi
doi: 10.1083/jcb.202006081
external_id:
isi:
- '000626365700001'
pmid:
- '33533935'
file:
- access_level: open_access
checksum: 843ebc153847c8626e13c9c5ce71d533
content_type: application/pdf
creator: dernst
date_created: 2022-05-12T14:16:21Z
date_updated: 2022-05-12T14:16:21Z
file_id: '11367'
file_name: 2021_JournCellBiology_Leithner.pdf
file_size: 5102328
relation: main_file
success: 1
file_date_updated: 2022-05-12T14:16:21Z
has_accepted_license: '1'
intvolume: ' 220'
isi: 1
issue: '4'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dendritic cell actin dynamics control contact duration and priming efficiency
at the immunological synapse
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 220
year: '2021'
...
---
_id: '9306'
abstract:
- lang: eng
text: Assemblies of actin and its regulators underlie the dynamic morphology of
all eukaryotic cells. To understand how actin regulatory proteins work together
to generate actin-rich structures such as filopodia, we analyzed the localization
of diverse actin regulators within filopodia in Drosophila embryos and in a complementary
in vitro system of filopodia-like structures (FLSs). We found that the composition
of the regulatory protein complex where actin is incorporated (the filopodial
tip complex) is remarkably heterogeneous both in vivo and in vitro. Our data reveal
that different pairs of proteins correlate with each other and with actin bundle
length, suggesting the presence of functional subcomplexes. This is consistent
with a theoretical framework where three or more redundant subcomplexes join the
tip complex stochastically, with any two being sufficient to drive filopodia formation.
We provide an explanation for the observed heterogeneity and suggest that a mechanism
based on multiple components allows stereotypical filopodial dynamics to arise
from diverse upstream signaling pathways.
acknowledgement: "This work was supported by European Research Council grant 281971,
Wellcome Trust Research Career Development Fellowship WT095829AIA and Wellcome Trust
Senior Research\r\nFellowship 219482/Z/19/Z to J.L. Gallop, a Wellcome Trust Senior
Investigator Award 098357 to B.D. Simons, and an Austrian Science Fund grant (P31639)
to E. Hannezo. We acknowledge\r\ncore funding by the Wellcome Trust (092096) and
Cancer Research UK (C6946/A14492). U. Dobramysl was supported by a Wellcome Trust
Junior Interdisciplinary Fellowship grant\r\n(105602/Z/14/Z) and a Herchel Smith
Postdoctoral Fellowship. H. Shimo was supported by a Funai Foundation Overseas scholarship."
article_number: e202003052
article_processing_charge: No
article_type: original
author:
- first_name: Ulrich
full_name: Dobramysl, Ulrich
last_name: Dobramysl
- first_name: Iris Katharina
full_name: Jarsch, Iris Katharina
last_name: Jarsch
- first_name: Yoshiko
full_name: Inoue, Yoshiko
last_name: Inoue
- first_name: Hanae
full_name: Shimo, Hanae
last_name: Shimo
- first_name: Benjamin
full_name: Richier, Benjamin
last_name: Richier
- first_name: Jonathan R.
full_name: Gadsby, Jonathan R.
last_name: Gadsby
- first_name: Julia
full_name: Mason, Julia
last_name: Mason
- first_name: Alicja
full_name: Szałapak, Alicja
last_name: Szałapak
- first_name: Pantelis Savvas
full_name: Ioannou, Pantelis Savvas
last_name: Ioannou
- first_name: Guilherme Pereira
full_name: Correia, Guilherme Pereira
last_name: Correia
- first_name: Astrid
full_name: Walrant, Astrid
last_name: Walrant
- first_name: Richard
full_name: Butler, Richard
last_name: Butler
- first_name: Edouard B
full_name: Hannezo, Edouard B
id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
last_name: Hannezo
orcid: 0000-0001-6005-1561
- first_name: Benjamin D.
full_name: Simons, Benjamin D.
last_name: Simons
- first_name: Jennifer L.
full_name: Gallop, Jennifer L.
last_name: Gallop
citation:
ama: Dobramysl U, Jarsch IK, Inoue Y, et al. Stochastic combinations of actin regulatory
proteins are sufficient to drive filopodia formation. Journal of Cell Biology.
2021;220(4). doi:10.1083/jcb.202003052
apa: Dobramysl, U., Jarsch, I. K., Inoue, Y., Shimo, H., Richier, B., Gadsby, J.
R., … Gallop, J. L. (2021). Stochastic combinations of actin regulatory proteins
are sufficient to drive filopodia formation. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.202003052
chicago: Dobramysl, Ulrich, Iris Katharina Jarsch, Yoshiko Inoue, Hanae Shimo, Benjamin
Richier, Jonathan R. Gadsby, Julia Mason, et al. “Stochastic Combinations of Actin
Regulatory Proteins Are Sufficient to Drive Filopodia Formation.” Journal of
Cell Biology. Rockefeller University Press, 2021. https://doi.org/10.1083/jcb.202003052.
ieee: U. Dobramysl et al., “Stochastic combinations of actin regulatory proteins
are sufficient to drive filopodia formation,” Journal of Cell Biology,
vol. 220, no. 4. Rockefeller University Press, 2021.
ista: Dobramysl U, Jarsch IK, Inoue Y, Shimo H, Richier B, Gadsby JR, Mason J, Szałapak
A, Ioannou PS, Correia GP, Walrant A, Butler R, Hannezo EB, Simons BD, Gallop
JL. 2021. Stochastic combinations of actin regulatory proteins are sufficient
to drive filopodia formation. Journal of Cell Biology. 220(4), e202003052.
mla: Dobramysl, Ulrich, et al. “Stochastic Combinations of Actin Regulatory Proteins
Are Sufficient to Drive Filopodia Formation.” Journal of Cell Biology,
vol. 220, no. 4, e202003052, Rockefeller University Press, 2021, doi:10.1083/jcb.202003052.
short: U. Dobramysl, I.K. Jarsch, Y. Inoue, H. Shimo, B. Richier, J.R. Gadsby, J.
Mason, A. Szałapak, P.S. Ioannou, G.P. Correia, A. Walrant, R. Butler, E.B. Hannezo,
B.D. Simons, J.L. Gallop, Journal of Cell Biology 220 (2021).
date_created: 2021-04-04T22:01:21Z
date_published: 2021-03-19T00:00:00Z
date_updated: 2026-04-02T13:59:43Z
day: '19'
ddc:
- '576'
department:
- _id: EdHa
doi: 10.1083/jcb.202003052
external_id:
isi:
- '000663160600002'
pmid:
- '33740033'
file:
- access_level: open_access
checksum: 4739ffd90f2c7e05ac5b00f057c58aa2
content_type: application/pdf
creator: dernst
date_created: 2021-04-06T10:39:08Z
date_updated: 2021-04-06T10:39:08Z
file_id: '9310'
file_name: 2021_JCB_Dobramysl.pdf
file_size: 9019720
relation: main_file
success: 1
file_date_updated: 2021-04-06T10:39:08Z
has_accepted_license: '1'
intvolume: ' 220'
isi: 1
issue: '4'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 268294B6-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31639
name: Active mechano-chemical description of the cell cytoskeleton
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Stochastic combinations of actin regulatory proteins are sufficient to drive
filopodia formation
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: 220
year: '2021'
...
---
_id: '7875'
abstract:
- lang: eng
text: 'Cells navigating through complex tissues face a fundamental challenge: while
multiple protrusions explore different paths, the cell needs to avoid entanglement.
How a cell surveys and then corrects its own shape is poorly understood. Here,
we demonstrate that spatially distinct microtubule dynamics regulate amoeboid
cell migration by locally promoting the retraction of protrusions. In migrating
dendritic cells, local microtubule depolymerization within protrusions remote
from the microtubule organizing center triggers actomyosin contractility controlled
by RhoA and its exchange factor Lfc. Depletion of Lfc leads to aberrant myosin
localization, thereby causing two effects that rate-limit locomotion: (1) impaired
cell edge coordination during path finding and (2) defective adhesion resolution.
Compromised shape control is particularly hindering in geometrically complex microenvironments,
where it leads to entanglement and ultimately fragmentation of the cell body.
We thus demonstrate that microtubules can act as a proprioceptive device: they
sense cell shape and control actomyosin retraction to sustain cellular coherence.'
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
- _id: PreCl
acknowledgement: "The authors thank the Scientific Service Units (Life Sciences, Bioimaging,
Preclinical) of the Institute of Science and Technology Austria for excellent support.
This work was funded by the European Research Council (ERC StG 281556 and CoG 724373),
two grants from the Austrian\r\nScience Fund (FWF; P29911 and DK Nanocell W1250-B20
to M. Sixt) and by the German Research Foundation (DFG SFB1032 project B09) to O.
Thorn-Seshold and D. Trauner. J. Renkawitz was supported by ISTFELLOW funding from
the People Program (Marie Curie Actions) of the European Union’s Seventh Framework
Programme (FP7/2007-2013) under the Research Executive Agency grant agreement (291734)
and a European Molecular Biology Organization long-term fellowship (ALTF 1396-2014)
co-funded by the European Commission (LTFCOFUND2013, GA-2013-609409), E. Kiermaier
by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s
Excellence Strategy—EXC 2151—390873048, and H. Hacker by the American Lebanese Syrian
Associated ¨Charities. K.-D. Fischer was supported by the Analysis, Imaging and
Modelling of Neuronal and Inflammatory Processes graduate school funded by the Ministry
of Economics, Science, and Digitisation of the State Saxony-Anhalt and by the European
Funds for Social and Regional Development."
article_number: e201907154
article_processing_charge: No
article_type: original
author:
- first_name: Aglaja
full_name: Kopf, Aglaja
id: 31DAC7B6-F248-11E8-B48F-1D18A9856A87
last_name: Kopf
orcid: 0000-0002-2187-6656
- first_name: Jörg
full_name: Renkawitz, Jörg
id: 3F0587C8-F248-11E8-B48F-1D18A9856A87
last_name: Renkawitz
orcid: 0000-0003-2856-3369
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
- first_name: Irute
full_name: Girkontaite, Irute
last_name: Girkontaite
- first_name: Kerry
full_name: Tedford, Kerry
last_name: Tedford
- first_name: Jack
full_name: Merrin, Jack
id: 4515C308-F248-11E8-B48F-1D18A9856A87
last_name: Merrin
orcid: 0000-0001-5145-4609
- first_name: Oliver
full_name: Thorn-Seshold, Oliver
last_name: Thorn-Seshold
- first_name: Dirk
full_name: Trauner, Dirk
id: E8F27F48-3EBA-11E9-92A1-B709E6697425
last_name: Trauner
- first_name: Hans
full_name: Häcker, Hans
last_name: Häcker
- first_name: Klaus Dieter
full_name: Fischer, Klaus Dieter
last_name: Fischer
- first_name: Eva
full_name: Kiermaier, Eva
id: 3EB04B78-F248-11E8-B48F-1D18A9856A87
last_name: Kiermaier
orcid: 0000-0001-6165-5738
- first_name: Michael K
full_name: Sixt, Michael K
id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
last_name: Sixt
orcid: 0000-0002-6620-9179
citation:
ama: Kopf A, Renkawitz J, Hauschild R, et al. Microtubules control cellular shape
and coherence in amoeboid migrating cells. The Journal of Cell Biology.
2020;219(6). doi:10.1083/jcb.201907154
apa: Kopf, A., Renkawitz, J., Hauschild, R., Girkontaite, I., Tedford, K., Merrin,
J., … Sixt, M. K. (2020). Microtubules control cellular shape and coherence in
amoeboid migrating cells. The Journal of Cell Biology. Rockefeller University
Press. https://doi.org/10.1083/jcb.201907154
chicago: Kopf, Aglaja, Jörg Renkawitz, Robert Hauschild, Irute Girkontaite, Kerry
Tedford, Jack Merrin, Oliver Thorn-Seshold, et al. “Microtubules Control Cellular
Shape and Coherence in Amoeboid Migrating Cells.” The Journal of Cell Biology.
Rockefeller University Press, 2020. https://doi.org/10.1083/jcb.201907154.
ieee: A. Kopf et al., “Microtubules control cellular shape and coherence
in amoeboid migrating cells,” The Journal of Cell Biology, vol. 219, no.
6. Rockefeller University Press, 2020.
ista: Kopf A, Renkawitz J, Hauschild R, Girkontaite I, Tedford K, Merrin J, Thorn-Seshold
O, Trauner D, Häcker H, Fischer KD, Kiermaier E, Sixt MK. 2020. Microtubules control
cellular shape and coherence in amoeboid migrating cells. The Journal of Cell
Biology. 219(6), e201907154.
mla: Kopf, Aglaja, et al. “Microtubules Control Cellular Shape and Coherence in
Amoeboid Migrating Cells.” The Journal of Cell Biology, vol. 219, no. 6,
e201907154, Rockefeller University Press, 2020, doi:10.1083/jcb.201907154.
short: A. Kopf, J. Renkawitz, R. Hauschild, I. Girkontaite, K. Tedford, J. Merrin,
O. Thorn-Seshold, D. Trauner, H. Häcker, K.D. Fischer, E. Kiermaier, M.K. Sixt,
The Journal of Cell Biology 219 (2020).
corr_author: '1'
date_created: 2020-05-24T22:00:56Z
date_published: 2020-06-01T00:00:00Z
date_updated: 2025-04-14T13:10:03Z
day: '01'
ddc:
- '570'
department:
- _id: MiSi
- _id: Bio
- _id: NanoFab
doi: 10.1083/jcb.201907154
ec_funded: 1
external_id:
isi:
- '000538141100020'
pmid:
- '32379884'
file:
- access_level: open_access
checksum: cb0b9c77842ae1214caade7b77e4d82d
content_type: application/pdf
creator: dernst
date_created: 2020-11-24T13:25:13Z
date_updated: 2020-11-24T13:25:13Z
file_id: '8801'
file_name: 2020_JCellBiol_Kopf.pdf
file_size: 7536712
relation: main_file
success: 1
file_date_updated: 2020-11-24T13:25:13Z
has_accepted_license: '1'
intvolume: ' 219'
isi: 1
issue: '6'
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 25A603A2-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '281556'
name: Cytoskeletal force generation and force transduction of migrating leukocytes
- _id: 25FE9508-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '724373'
name: Cellular Navigation Along Spatial Gradients
- _id: 26018E70-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P29911
name: Mechanical adaptation of lamellipodial actin
- _id: 252C3B08-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: W1250-B20
name: Nano-Analytics of Cellular Systems
- _id: 25681D80-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '291734'
name: International IST Postdoc Fellowship Programme
- _id: 25A48D24-B435-11E9-9278-68D0E5697425
grant_number: ALTF 1396-2014
name: Molecular and system level view of immune cell migration
publication: The Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Microtubules control cellular shape and coherence in amoeboid migrating cells
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: 219
year: '2020'
...
---
_id: '8190'
article_number: e202007029
article_processing_charge: No
article_type: letter_note
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: Anna
full_name: Huttenlocher, Anna
last_name: Huttenlocher
citation:
ama: 'Sixt MK, Huttenlocher A. Zena Werb (1945-2020): Cell biology in context. The
Journal of Cell Biology. 2020;219(8). doi:10.1083/jcb.202007029'
apa: 'Sixt, M. K., & Huttenlocher, A. (2020). Zena Werb (1945-2020): Cell biology
in context. The Journal of Cell Biology. Rockefeller University Press.
https://doi.org/10.1083/jcb.202007029'
chicago: 'Sixt, Michael K, and Anna Huttenlocher. “Zena Werb (1945-2020): Cell Biology
in Context.” The Journal of Cell Biology. Rockefeller University Press,
2020. https://doi.org/10.1083/jcb.202007029.'
ieee: 'M. K. Sixt and A. Huttenlocher, “Zena Werb (1945-2020): Cell biology in context,”
The Journal of Cell Biology, vol. 219, no. 8. Rockefeller University Press,
2020.'
ista: 'Sixt MK, Huttenlocher A. 2020. Zena Werb (1945-2020): Cell biology in context.
The Journal of Cell Biology. 219(8), e202007029.'
mla: 'Sixt, Michael K., and Anna Huttenlocher. “Zena Werb (1945-2020): Cell Biology
in Context.” The Journal of Cell Biology, vol. 219, no. 8, e202007029,
Rockefeller University Press, 2020, doi:10.1083/jcb.202007029.'
short: M.K. Sixt, A. Huttenlocher, The Journal of Cell Biology 219 (2020).
date_created: 2020-08-02T22:00:57Z
date_published: 2020-07-22T00:00:00Z
date_updated: 2025-06-12T07:34:40Z
day: '22'
ddc:
- '570'
department:
- _id: MiSi
doi: 10.1083/jcb.202007029
external_id:
isi:
- '000573631000004'
pmid:
- '32699885'
file:
- access_level: open_access
checksum: 30016d778d266b8e17d01094917873b8
content_type: application/pdf
creator: dernst
date_created: 2020-08-04T13:11:52Z
date_updated: 2021-02-02T23:30:03Z
embargo: 2021-02-01
file_id: '8200'
file_name: 2020_JCB_Sixt.pdf
file_size: 830725
relation: main_file
file_date_updated: 2021-02-02T23:30:03Z
has_accepted_license: '1'
intvolume: ' 219'
isi: 1
issue: '8'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: The Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
publication_status: published
publisher: Rockefeller University Press
scopus_import: '1'
status: public
title: 'Zena Werb (1945-2020): Cell biology in context'
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 219
year: '2020'
...
---
_id: '11061'
abstract:
- lang: eng
text: Many adult tissues contain postmitotic cells as old as the host organism.
The only organelle that does not turn over in these cells is the nucleus, and
its maintenance represents a formidable challenge, as it harbors regulatory proteins
that persist throughout adulthood. Here we developed strategies to visualize two
classes of such long-lived proteins, histones and nucleoporins, to understand
the function of protein longevity in nuclear maintenance. Genome-wide mapping
of histones revealed specific enrichment of long-lived variants at silent gene
loci. Interestingly, nuclear pores are maintained by piecemeal replacement of
subunits, resulting in mosaic complexes composed of polypeptides with vastly different
ages. In contrast, nondividing quiescent cells remove old nuclear pores in an
ESCRT-dependent manner. Our findings reveal distinct molecular strategies of nuclear
maintenance, linking lifelong protein persistence to gene regulation and nuclear
integrity.
article_processing_charge: No
article_type: original
author:
- first_name: Brandon H.
full_name: Toyama, Brandon H.
last_name: Toyama
- first_name: Rafael
full_name: Arrojo e Drigo, Rafael
last_name: Arrojo e Drigo
- first_name: Varda
full_name: Lev-Ram, Varda
last_name: Lev-Ram
- first_name: Ranjan
full_name: Ramachandra, Ranjan
last_name: Ramachandra
- first_name: Thomas J.
full_name: Deerinck, Thomas J.
last_name: Deerinck
- first_name: Claude
full_name: Lechene, Claude
last_name: Lechene
- first_name: Mark H.
full_name: Ellisman, Mark H.
last_name: Ellisman
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Toyama BH, Arrojo e Drigo R, Lev-Ram V, et al. Visualization of long-lived
proteins reveals age mosaicism within nuclei of postmitotic cells. Journal
of Cell Biology. 2019;218(2):433-444. doi:10.1083/jcb.201809123
apa: Toyama, B. H., Arrojo e Drigo, R., Lev-Ram, V., Ramachandra, R., Deerinck,
T. J., Lechene, C., … Hetzer, M. (2019). Visualization of long-lived proteins
reveals age mosaicism within nuclei of postmitotic cells. Journal of Cell Biology.
Rockefeller University Press. https://doi.org/10.1083/jcb.201809123
chicago: Toyama, Brandon H., Rafael Arrojo e Drigo, Varda Lev-Ram, Ranjan Ramachandra,
Thomas J. Deerinck, Claude Lechene, Mark H. Ellisman, and Martin Hetzer. “Visualization
of Long-Lived Proteins Reveals Age Mosaicism within Nuclei of Postmitotic Cells.”
Journal of Cell Biology. Rockefeller University Press, 2019. https://doi.org/10.1083/jcb.201809123.
ieee: B. H. Toyama et al., “Visualization of long-lived proteins reveals
age mosaicism within nuclei of postmitotic cells,” Journal of Cell Biology,
vol. 218, no. 2. Rockefeller University Press, pp. 433–444, 2019.
ista: Toyama BH, Arrojo e Drigo R, Lev-Ram V, Ramachandra R, Deerinck TJ, Lechene
C, Ellisman MH, Hetzer M. 2019. Visualization of long-lived proteins reveals age
mosaicism within nuclei of postmitotic cells. Journal of Cell Biology. 218(2),
433–444.
mla: Toyama, Brandon H., et al. “Visualization of Long-Lived Proteins Reveals Age
Mosaicism within Nuclei of Postmitotic Cells.” Journal of Cell Biology,
vol. 218, no. 2, Rockefeller University Press, 2019, pp. 433–44, doi:10.1083/jcb.201809123.
short: B.H. Toyama, R. Arrojo e Drigo, V. Lev-Ram, R. Ramachandra, T.J. Deerinck,
C. Lechene, M.H. Ellisman, M. Hetzer, Journal of Cell Biology 218 (2019) 433–444.
date_created: 2022-04-07T07:45:11Z
date_published: 2019-02-04T00:00:00Z
date_updated: 2024-10-14T11:19:21Z
day: '04'
ddc:
- '570'
doi: 10.1083/jcb.201809123
extern: '1'
external_id:
pmid:
- '30552100'
file:
- access_level: open_access
checksum: 7964ebbf833b0b35f9fba840eea9531d
content_type: application/pdf
creator: dernst
date_created: 2022-04-08T08:26:32Z
date_updated: 2022-04-08T08:26:32Z
file_id: '11139'
file_name: 2019_JCB_Toyama.pdf
file_size: 2503838
relation: main_file
success: 1
file_date_updated: 2022-04-08T08:26:32Z
has_accepted_license: '1'
intvolume: ' 218'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 433-444
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Visualization of long-lived proteins reveals age mosaicism within nuclei of
postmitotic cells
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 218
year: '2019'
...
---
_id: '11075'
abstract:
- lang: eng
text: Previously, we identified the nucleoporin gp210/Nup210 as a critical regulator
of muscle and neuronal differentiation, but how this nucleoporin exerts its function
and whether it modulates nuclear pore complex (NPC) activity remain unknown. Here,
we show that gp210/Nup210 mediates muscle cell differentiation in vitro via its
conserved N-terminal domain that extends into the perinuclear space. Removal of
the C-terminal domain, which partially mislocalizes gp210/Nup210 away from NPCs,
efficiently rescues the differentiation defect caused by the knockdown of endogenous
gp210/Nup210. Unexpectedly, a gp210/Nup210 mutant lacking the NPC-targeting transmembrane
and C-terminal domains is sufficient for C2C12 myoblast differentiation. We demonstrate
that the endoplasmic reticulum (ER) stress-specific caspase cascade is exacerbated
during Nup210 depletion and that blocking ER stress-mediated apoptosis rescues
differentiation of Nup210-deficient cells. Our results suggest that the role of
gp210/Nup210 in cell differentiation is mediated by its large luminal domain,
which can act independently of NPC association and appears to play a pivotal role
in the maintenance of nuclear envelope/ER homeostasis.
article_processing_charge: No
article_type: original
author:
- first_name: J. Sebastian
full_name: Gomez-Cavazos, J. Sebastian
last_name: Gomez-Cavazos
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Gomez-Cavazos JS, Hetzer M. The nucleoporin gp210/Nup210 controls muscle differentiation
by regulating nuclear envelope/ER homeostasis. Journal of Cell Biology.
2015;208(6):671-681. doi:10.1083/jcb.201410047
apa: Gomez-Cavazos, J. S., & Hetzer, M. (2015). The nucleoporin gp210/Nup210
controls muscle differentiation by regulating nuclear envelope/ER homeostasis.
Journal of Cell Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.201410047
chicago: Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210
Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.”
Journal of Cell Biology. Rockefeller University Press, 2015. https://doi.org/10.1083/jcb.201410047.
ieee: J. S. Gomez-Cavazos and M. Hetzer, “The nucleoporin gp210/Nup210 controls
muscle differentiation by regulating nuclear envelope/ER homeostasis,” Journal
of Cell Biology, vol. 208, no. 6. Rockefeller University Press, pp. 671–681,
2015.
ista: Gomez-Cavazos JS, Hetzer M. 2015. The nucleoporin gp210/Nup210 controls muscle
differentiation by regulating nuclear envelope/ER homeostasis. Journal of Cell
Biology. 208(6), 671–681.
mla: Gomez-Cavazos, J. Sebastian, and Martin Hetzer. “The Nucleoporin Gp210/Nup210
Controls Muscle Differentiation by Regulating Nuclear Envelope/ER Homeostasis.”
Journal of Cell Biology, vol. 208, no. 6, Rockefeller University Press,
2015, pp. 671–81, doi:10.1083/jcb.201410047.
short: J.S. Gomez-Cavazos, M. Hetzer, Journal of Cell Biology 208 (2015) 671–681.
date_created: 2022-04-07T07:49:10Z
date_published: 2015-03-16T00:00:00Z
date_updated: 2024-10-14T11:22:26Z
day: '16'
doi: 10.1083/jcb.201410047
extern: '1'
external_id:
pmid:
- '25778917'
intvolume: ' 208'
issue: '6'
keyword:
- Cell Biology
language:
- iso: eng
month: '03'
oa_version: Published Version
page: 671-681
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: The nucleoporin gp210/Nup210 controls muscle differentiation by regulating
nuclear envelope/ER homeostasis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 208
year: '2015'
...
---
_id: '11094'
abstract:
- lang: eng
text: Nuclear pore complexes (NPCs) assemble at the end of mitosis during nuclear
envelope (NE) reformation and into an intact NE as cells progress through interphase.
Although recent studies have shown that NPC formation occurs by two different
molecular mechanisms at two distinct cell cycle stages, little is known about
the molecular players that mediate the fusion of the outer and inner nuclear membranes
to form pores. In this paper, we provide evidence that the transmembrane nucleoporin
(Nup), POM121, but not the Nup107–160 complex, is present at new pore assembly
sites at a time that coincides with inner nuclear membrane (INM) and outer nuclear
membrane (ONM) fusion. Overexpression of POM121 resulted in juxtaposition of the
INM and ONM. Additionally, Sun1, an INM protein that is known to interact with
the cytoskeleton, was specifically required for interphase assembly and localized
with POM121 at forming pores. We propose a model in which POM121 and Sun1 interact
transiently to promote early steps of interphase NPC assembly.
article_processing_charge: No
article_type: original
author:
- first_name: Jessica A.
full_name: Talamas, Jessica A.
last_name: Talamas
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Talamas JA, Hetzer M. POM121 and Sun1 play a role in early steps of interphase
NPC assembly. Journal of Cell Biology. 2011;194(1):27-37. doi:10.1083/jcb.201012154
apa: Talamas, J. A., & Hetzer, M. (2011). POM121 and Sun1 play a role in early
steps of interphase NPC assembly. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.201012154
chicago: Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in
Early Steps of Interphase NPC Assembly.” Journal of Cell Biology. Rockefeller
University Press, 2011. https://doi.org/10.1083/jcb.201012154.
ieee: J. A. Talamas and M. Hetzer, “POM121 and Sun1 play a role in early steps of
interphase NPC assembly,” Journal of Cell Biology, vol. 194, no. 1. Rockefeller
University Press, pp. 27–37, 2011.
ista: Talamas JA, Hetzer M. 2011. POM121 and Sun1 play a role in early steps of
interphase NPC assembly. Journal of Cell Biology. 194(1), 27–37.
mla: Talamas, Jessica A., and Martin Hetzer. “POM121 and Sun1 Play a Role in Early
Steps of Interphase NPC Assembly.” Journal of Cell Biology, vol. 194, no.
1, Rockefeller University Press, 2011, pp. 27–37, doi:10.1083/jcb.201012154.
short: J.A. Talamas, M. Hetzer, Journal of Cell Biology 194 (2011) 27–37.
date_created: 2022-04-07T07:52:18Z
date_published: 2011-07-04T00:00:00Z
date_updated: 2024-10-14T11:26:10Z
day: '04'
doi: 10.1083/jcb.201012154
extern: '1'
external_id:
pmid:
- '21727197'
intvolume: ' 194'
issue: '1'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.201012154
month: '07'
oa: 1
oa_version: Published Version
page: 27-37
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: POM121 and Sun1 play a role in early steps of interphase NPC assembly
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 194
year: '2011'
...
---
_id: '11106'
abstract:
- lang: eng
text: Formation of the nuclear envelope (NE) around segregated chromosomes occurs
by the reshaping of the endoplasmic reticulum (ER), a reservoir for disassembled
nuclear membrane components during mitosis. In this study, we show that inner
nuclear membrane proteins such as lamin B receptor (LBR), MAN1, Lap2β, and the
trans-membrane nucleoporins Ndc1 and POM121 drive the spreading of ER membranes
into the emerging NE via their capacity to bind chromatin in a collaborative manner.
Despite their redundant functions, decreasing the levels of any of these trans-membrane
proteins by RNAi-mediated knockdown delayed NE formation, whereas increasing the
levels of any of them had the opposite effect. Furthermore, acceleration of NE
formation interferes with chromosome separation during mitosis, indicating that
the time frame over which chromatin becomes membrane enclosed is physiologically
relevant and regulated. These data suggest that functionally distinct classes
of chromatin-interacting membrane proteins, which are present at nonsaturating
levels, collaborate to rapidly reestablish the nuclear compartment at the end
of mitosis.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Jesse D.
full_name: Vargas, Jesse D.
last_name: Vargas
- first_name: Joshua P.
full_name: Hsiao, Joshua P.
last_name: Hsiao
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. Recruitment of functionally distinct
membrane proteins to chromatin mediates nuclear envelope formation in vivo. Journal
of Cell Biology. 2009;186(2):183-191. doi:10.1083/jcb.200901106
apa: Anderson, D. J., Vargas, J. D., Hsiao, J. P., & Hetzer, M. (2009). Recruitment
of functionally distinct membrane proteins to chromatin mediates nuclear envelope
formation in vivo. Journal of Cell Biology. Rockefeller University Press.
https://doi.org/10.1083/jcb.200901106
chicago: Anderson, Daniel J., Jesse D. Vargas, Joshua P. Hsiao, and Martin Hetzer.
“Recruitment of Functionally Distinct Membrane Proteins to Chromatin Mediates
Nuclear Envelope Formation in Vivo.” Journal of Cell Biology. Rockefeller
University Press, 2009. https://doi.org/10.1083/jcb.200901106.
ieee: D. J. Anderson, J. D. Vargas, J. P. Hsiao, and M. Hetzer, “Recruitment of
functionally distinct membrane proteins to chromatin mediates nuclear envelope
formation in vivo,” Journal of Cell Biology, vol. 186, no. 2. Rockefeller
University Press, pp. 183–191, 2009.
ista: Anderson DJ, Vargas JD, Hsiao JP, Hetzer M. 2009. Recruitment of functionally
distinct membrane proteins to chromatin mediates nuclear envelope formation in
vivo. Journal of Cell Biology. 186(2), 183–191.
mla: Anderson, Daniel J., et al. “Recruitment of Functionally Distinct Membrane
Proteins to Chromatin Mediates Nuclear Envelope Formation in Vivo.” Journal
of Cell Biology, vol. 186, no. 2, Rockefeller University Press, 2009, pp.
183–91, doi:10.1083/jcb.200901106.
short: D.J. Anderson, J.D. Vargas, J.P. Hsiao, M. Hetzer, Journal of Cell Biology
186 (2009) 183–191.
date_created: 2022-04-07T07:54:18Z
date_published: 2009-07-20T00:00:00Z
date_updated: 2024-10-14T11:28:48Z
day: '20'
doi: 10.1083/jcb.200901106
extern: '1'
external_id:
pmid:
- '19620630'
intvolume: ' 186'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.200901106
month: '07'
oa: 1
oa_version: Published Version
page: 183-191
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1083/jcb.20090110620090903c
scopus_import: '1'
status: public
title: Recruitment of functionally distinct membrane proteins to chromatin mediates
nuclear envelope formation in vivo
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 186
year: '2009'
...
---
_id: '11107'
abstract:
- lang: eng
text: Nucleocytoplasmic transport occurs exclusively through nuclear pore complexes
(NPCs) embedded in pores formed by inner and outer nuclear membrane fusion. The
mechanism for de novo pore and NPC biogenesis remains unclear. Reticulons (RTNs)
and Yop1/DP1 are conserved membrane protein families required to form and maintain
the tubular endoplasmic reticulum (ER) and the postmitotic nuclear envelope. In
this study, we report that members of the RTN and Yop1/DP1 families are required
for nuclear pore formation. Analysis of Saccharomyces cerevisiae prp20-G282S and
nup133Δ NPC assembly mutants revealed perturbations in Rtn1–green fluorescent
protein (GFP) and Yop1-GFP ER distribution and colocalization to NPC clusters.
Combined deletion of RTN1 and YOP1 resulted in NPC clustering, nuclear import
defects, and synthetic lethality with the additional absence of Pom34, Pom152,
and Nup84 subcomplex members. We tested for a direct role in NPC biogenesis using
Xenopus laevis in vitro assays and found that anti-Rtn4a antibodies specifically
inhibited de novo nuclear pore formation. We hypothesize that these ER membrane–bending
proteins mediate early NPC assembly steps.
article_processing_charge: No
article_type: original
author:
- first_name: T. Renee
full_name: Dawson, T. Renee
last_name: Dawson
- first_name: Michelle D.
full_name: Lazarus, Michelle D.
last_name: Lazarus
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
- first_name: Susan R.
full_name: Wente, Susan R.
last_name: Wente
citation:
ama: Dawson TR, Lazarus MD, Hetzer M, Wente SR. ER membrane–bending proteins are
necessary for de novo nuclear pore formation. Journal of Cell Biology.
2009;184(5):659-675. doi:10.1083/jcb.200806174
apa: Dawson, T. R., Lazarus, M. D., Hetzer, M., & Wente, S. R. (2009). ER membrane–bending
proteins are necessary for de novo nuclear pore formation. Journal of Cell
Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.200806174
chicago: Dawson, T. Renee, Michelle D. Lazarus, Martin Hetzer, and Susan R. Wente.
“ER Membrane–Bending Proteins Are Necessary for de Novo Nuclear Pore Formation.”
Journal of Cell Biology. Rockefeller University Press, 2009. https://doi.org/10.1083/jcb.200806174.
ieee: T. R. Dawson, M. D. Lazarus, M. Hetzer, and S. R. Wente, “ER membrane–bending
proteins are necessary for de novo nuclear pore formation,” Journal of Cell
Biology, vol. 184, no. 5. Rockefeller University Press, pp. 659–675, 2009.
ista: Dawson TR, Lazarus MD, Hetzer M, Wente SR. 2009. ER membrane–bending proteins
are necessary for de novo nuclear pore formation. Journal of Cell Biology. 184(5),
659–675.
mla: Dawson, T. Renee, et al. “ER Membrane–Bending Proteins Are Necessary for de
Novo Nuclear Pore Formation.” Journal of Cell Biology, vol. 184, no. 5,
Rockefeller University Press, 2009, pp. 659–75, doi:10.1083/jcb.200806174.
short: T.R. Dawson, M.D. Lazarus, M. Hetzer, S.R. Wente, Journal of Cell Biology
184 (2009) 659–675.
date_created: 2022-04-07T07:54:44Z
date_published: 2009-03-09T00:00:00Z
date_updated: 2022-07-18T08:55:05Z
day: '09'
doi: 10.1083/jcb.200806174
extern: '1'
external_id:
pmid:
- '19273614'
intvolume: ' 184'
issue: '5'
keyword:
- Cell Biology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1083/jcb.200806174
month: '03'
oa: 1
oa_version: Published Version
page: 659-675
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: ER membrane–bending proteins are necessary for de novo nuclear pore formation
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 184
year: '2009'
...
---
_id: '11111'
abstract:
- lang: eng
text: During mitosis in metazoans, segregated chromosomes become enclosed by the
nuclear envelope (NE), a double membrane that is continuous with the endoplasmic
reticulum (ER). Recent in vitro data suggest that NE formation occurs by chromatin-mediated
reorganization of the tubular ER; however, the basic principles of such a membrane-reshaping
process remain uncharacterized. Here, we present a quantitative analysis of nuclear
membrane assembly in mammalian cells using time-lapse microscopy. From the initial
recruitment of ER tubules to chromatin, the formation of a membrane-enclosed,
transport-competent nucleus occurs within ∼12 min. Overexpression of the ER tubule-forming
proteins reticulon 3, reticulon 4, and DP1 inhibits NE formation and nuclear expansion,
whereas their knockdown accelerates nuclear assembly. This suggests that the transition
from membrane tubules to sheets is rate-limiting for nuclear assembly. Our results
provide evidence that ER-shaping proteins are directly involved in the reconstruction
of the nuclear compartment and that morphological restructuring of the ER is the
principal mechanism of NE formation in vivo.
article_processing_charge: No
article_type: original
author:
- first_name: Daniel J.
full_name: Anderson, Daniel J.
last_name: Anderson
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
citation:
ama: Anderson DJ, Hetzer M. Reshaping of the endoplasmic reticulum limits the rate
for nuclear envelope formation. Journal of Cell Biology. 2008;182(5):911-924.
doi:10.1083/jcb.200805140
apa: Anderson, D. J., & Hetzer, M. (2008). Reshaping of the endoplasmic reticulum
limits the rate for nuclear envelope formation. Journal of Cell Biology.
Rockefeller University Press. https://doi.org/10.1083/jcb.200805140
chicago: Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum
Limits the Rate for Nuclear Envelope Formation.” Journal of Cell Biology.
Rockefeller University Press, 2008. https://doi.org/10.1083/jcb.200805140.
ieee: D. J. Anderson and M. Hetzer, “Reshaping of the endoplasmic reticulum limits
the rate for nuclear envelope formation,” Journal of Cell Biology, vol.
182, no. 5. Rockefeller University Press, pp. 911–924, 2008.
ista: Anderson DJ, Hetzer M. 2008. Reshaping of the endoplasmic reticulum limits
the rate for nuclear envelope formation. Journal of Cell Biology. 182(5), 911–924.
mla: Anderson, Daniel J., and Martin Hetzer. “Reshaping of the Endoplasmic Reticulum
Limits the Rate for Nuclear Envelope Formation.” Journal of Cell Biology,
vol. 182, no. 5, Rockefeller University Press, 2008, pp. 911–24, doi:10.1083/jcb.200805140.
short: D.J. Anderson, M. Hetzer, Journal of Cell Biology 182 (2008) 911–924.
date_created: 2022-04-07T07:55:23Z
date_published: 2008-09-08T00:00:00Z
date_updated: 2024-10-14T11:29:29Z
day: '08'
doi: 10.1083/jcb.200805140
extern: '1'
external_id:
pmid:
- '18779370'
intvolume: ' 182'
issue: '5'
keyword:
- Cell Biology
language:
- iso: eng
month: '09'
oa_version: None
page: 911-924
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope
formation
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 182
year: '2008'
...
---
_id: '11126'
abstract:
- lang: eng
text: Nuclear import of the two uracil-rich small nuclear ribonucleoprotein (U snRNP)
components U1A and U2B′′ is mediated by unusually long and complex nuclear localization
signals (NLSs). Here we investigate nuclear import of U1A and U2B′′ in vitro and
demonstrate that it occurs by an active, saturable process. Several lines of evidence
suggest that import of the two proteins occurs by an import mechanism different
to those characterized previously. No cross competition is seen with a variety
of previously studied NLSs. In contrast to import mediated by members of the importin-β
family of nucleocytoplasmic transport receptors, U1A/U2B′′ import is not inhibited
by either nonhydrolyzable guanosine triphosphate (GTP) analogues or by a mutant
of the GTPase Ran that is incapable of GTP hydrolysis. Adenosine triphosphate
is capable of supporting U1A and U2B′′ import, whereas neither nonhydrolyzable
adenosine triphosphate analogues nor GTP can do so. U1A and U2B′′ import in vitro
does not require the addition of soluble cytosolic proteins, but a factor or factors
required for U1A and U2B′′ import remains tightly associated with the nuclear
fraction of conventionally permeabilized cells. This activity can be solubilized
in the presence of elevated MgCl2. These data suggest that U1A and U2B′′ import
into the nucleus occurs by a hitherto uncharacterized mechanism.
article_processing_charge: No
article_type: original
author:
- first_name: Martin W
full_name: HETZER, Martin W
id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
last_name: HETZER
orcid: 0000-0002-2111-992X
- first_name: Iain W.
full_name: Mattaj, Iain W.
last_name: Mattaj
citation:
ama: Hetzer M, Mattaj IW. An Atp-dependent, Ran-independent mechanism for nuclear
import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology.
2000;148(2):293-304. doi:10.1083/jcb.148.2.293
apa: Hetzer, M., & Mattaj, I. W. (2000). An Atp-dependent, Ran-independent mechanism
for nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell
Biology. Rockefeller University Press. https://doi.org/10.1083/jcb.148.2.293
chicago: Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent
Mechanism for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” Journal
of Cell Biology. Rockefeller University Press, 2000. https://doi.org/10.1083/jcb.148.2.293.
ieee: M. Hetzer and I. W. Mattaj, “An Atp-dependent, Ran-independent mechanism for
nuclear import of the U1a and U2b′′ spliceosome proteins,” Journal of Cell
Biology, vol. 148, no. 2. Rockefeller University Press, pp. 293–304, 2000.
ista: Hetzer M, Mattaj IW. 2000. An Atp-dependent, Ran-independent mechanism for
nuclear import of the U1a and U2b′′ spliceosome proteins. Journal of Cell Biology.
148(2), 293–304.
mla: Hetzer, Martin, and Iain W. Mattaj. “An Atp-Dependent, Ran-Independent Mechanism
for Nuclear Import of the U1a and U2b′′ Spliceosome Proteins.” Journal of Cell
Biology, vol. 148, no. 2, Rockefeller University Press, 2000, pp. 293–304,
doi:10.1083/jcb.148.2.293.
short: M. Hetzer, I.W. Mattaj, Journal of Cell Biology 148 (2000) 293–304.
date_created: 2022-04-07T07:57:49Z
date_published: 2000-01-24T00:00:00Z
date_updated: 2022-07-18T08:58:29Z
day: '24'
doi: 10.1083/jcb.148.2.293
extern: '1'
external_id:
pmid:
- '10648562'
intvolume: ' 148'
issue: '2'
keyword:
- Cell Biology
language:
- iso: eng
month: '01'
oa_version: None
page: 293-304
pmid: 1
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: An Atp-dependent, Ran-independent mechanism for nuclear import of the U1a and
U2b′′ spliceosome proteins
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 148
year: '2000'
...