---
_id: '11060'
abstract:
- lang: eng
  text: The inner nuclear membrane (INM) is a subdomain of the endoplasmic reticulum
    (ER) that is gated by the nuclear pore complex. It is unknown whether proteins
    of the INM and ER are degraded through shared or distinct pathways in mammalian
    cells. We applied dynamic proteomics to profile protein half-lives and report
    that INM and ER residents turn over at similar rates, indicating that the INM’s
    unique topology is not a barrier to turnover. Using a microscopy approach, we
    observed that the proteasome can degrade INM proteins in situ. However, we also
    uncovered evidence for selective, vesicular transport-mediated turnover of a single
    INM protein, emerin, that is potentiated by ER stress. Emerin is rapidly cleared
    from the INM by a mechanism that requires emerin’s LEM domain to mediate vesicular
    trafficking to lysosomes. This work demonstrates that the INM can be dynamically
    remodeled in response to environmental inputs.
article_number: e49796
article_processing_charge: No
article_type: original
author:
- first_name: Abigail
  full_name: Buchwalter, Abigail
  last_name: Buchwalter
- first_name: Roberta
  full_name: Schulte, Roberta
  last_name: Schulte
- first_name: Hsiao
  full_name: Tsai, Hsiao
  last_name: Tsai
- first_name: Juliana
  full_name: Capitanio, Juliana
  last_name: Capitanio
- 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: Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. Selective clearance
    of the inner nuclear membrane protein emerin by vesicular transport during ER
    stress. <i>eLife</i>. 2019;8. doi:<a href="https://doi.org/10.7554/elife.49796">10.7554/elife.49796</a>
  apa: Buchwalter, A., Schulte, R., Tsai, H., Capitanio, J., &#38; Hetzer, M. (2019).
    Selective clearance of the inner nuclear membrane protein emerin by vesicular
    transport during ER stress. <i>ELife</i>. eLife Sciences Publications. <a href="https://doi.org/10.7554/elife.49796">https://doi.org/10.7554/elife.49796</a>
  chicago: Buchwalter, Abigail, Roberta Schulte, Hsiao Tsai, Juliana Capitanio, and
    Martin Hetzer. “Selective Clearance of the Inner Nuclear Membrane Protein Emerin
    by Vesicular Transport during ER Stress.” <i>ELife</i>. eLife Sciences Publications,
    2019. <a href="https://doi.org/10.7554/elife.49796">https://doi.org/10.7554/elife.49796</a>.
  ieee: A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective
    clearance of the inner nuclear membrane protein emerin by vesicular transport
    during ER stress,” <i>eLife</i>, vol. 8. eLife Sciences Publications, 2019.
  ista: Buchwalter A, Schulte R, Tsai H, Capitanio J, Hetzer M. 2019. Selective clearance
    of the inner nuclear membrane protein emerin by vesicular transport during ER
    stress. eLife. 8, e49796.
  mla: Buchwalter, Abigail, et al. “Selective Clearance of the Inner Nuclear Membrane
    Protein Emerin by Vesicular Transport during ER Stress.” <i>ELife</i>, vol. 8,
    e49796, eLife Sciences Publications, 2019, doi:<a href="https://doi.org/10.7554/elife.49796">10.7554/elife.49796</a>.
  short: A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, M. Hetzer, ELife 8 (2019).
date_created: 2022-04-07T07:45:02Z
date_published: 2019-10-10T00:00:00Z
date_updated: 2024-10-14T12:08:36Z
day: '10'
ddc:
- '570'
doi: 10.7554/elife.49796
extern: '1'
external_id:
  pmid:
  - '31599721'
file:
- access_level: open_access
  checksum: 1e8672a1e9c3dc0a2d3d0dad89673616
  content_type: application/pdf
  creator: dernst
  date_created: 2022-04-08T08:18:01Z
  date_updated: 2022-04-08T08:18:01Z
  file_id: '11138'
  file_name: 2019_eLife_Buchwalter.pdf
  file_size: 6984654
  relation: main_file
  success: 1
file_date_updated: 2022-04-08T08:18:01Z
fulldoi: https://doi.org/10.7554/elife.49796
has_accepted_license: '1'
intvolume: '         8'
keyword:
- General Immunology and Microbiology
- General Biochemistry
- Genetics and Molecular Biology
- General Medicine
- General Neuroscience
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: eLife
publication_identifier:
  issn:
  - 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
related_material:
  record:
  - id: '13079'
    relation: research_data
    status: public
scopus_import: '1'
status: public
title: Selective clearance of the inner nuclear membrane protein emerin by vesicular
  transport during ER stress
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: 8
year: '2019'
...
---
_id: '12192'
abstract:
- lang: eng
  text: Transposable elements (TEs), the movement of which can damage the genome,
    are epigenetically silenced in eukaryotes. Intriguingly, TEs are activated in
    the sperm companion cell – vegetative cell (VC) – of the flowering plant Arabidopsis
    thaliana. However, the extent and mechanism of this activation are unknown. Here
    we show that about 100 heterochromatic TEs are activated in VCs, mostly by DEMETER-catalyzed
    DNA demethylation. We further demonstrate that DEMETER access to some of these
    TEs is permitted by the natural depletion of linker histone H1 in VCs. Ectopically
    expressed H1 suppresses TEs in VCs by reducing DNA demethylation and via a methylation-independent
    mechanism. We demonstrate that H1 is required for heterochromatin condensation
    in plant cells and show that H1 overexpression creates heterochromatic foci in
    the VC progenitor cell. Taken together, our results demonstrate that the natural
    depletion of H1 during male gametogenesis facilitates DEMETER-directed DNA demethylation,
    heterochromatin relaxation, and TE activation.
acknowledgement: We thank David Twell for the pDONR-P4-P1R-pLAT52 and pDONR-P2R-P3-mRFP
  vectors, the John Innes Centre Bioimaging Facility (Elaine Barclay and Grant Calder)
  for their assistance with microscopy, and the Norwich BioScience Institute Partnership
  Computing infrastructure for Science Group for High Performance Computing resources.
  This work was funded by a Biotechnology and Biological Sciences Research Council
  (BBSRC) David Phillips Fellowship (BB/L025043/1; SH, JZ and XF), a European Research
  Council Starting Grant ('SexMeth' 804981; XF) and a Grant to Exceptional Researchers
  by the Gatsby Charitable Foundation (SH and XF).
article_number: '42530'
article_processing_charge: No
article_type: original
author:
- first_name: Shengbo
  full_name: He, Shengbo
  last_name: He
- first_name: Martin
  full_name: Vickers, Martin
  last_name: Vickers
- first_name: Jingyi
  full_name: Zhang, Jingyi
  last_name: Zhang
- first_name: Xiaoqi
  full_name: Feng, Xiaoqi
  id: e0164712-22ee-11ed-b12a-d80fcdf35958
  last_name: Feng
  orcid: 0000-0002-4008-1234
citation:
  ama: He S, Vickers M, Zhang J, Feng X. Natural depletion of histone H1 in sex cells
    causes DNA demethylation, heterochromatin decondensation and transposon activation.
    <i>eLife</i>. 2019;8. doi:<a href="https://doi.org/10.7554/elife.42530">10.7554/elife.42530</a>
  apa: He, S., Vickers, M., Zhang, J., &#38; Feng, X. (2019). Natural depletion of
    histone H1 in sex cells causes DNA demethylation, heterochromatin decondensation
    and transposon activation. <i>ELife</i>. eLife Sciences Publications. <a href="https://doi.org/10.7554/elife.42530">https://doi.org/10.7554/elife.42530</a>
  chicago: He, Shengbo, Martin Vickers, Jingyi Zhang, and Xiaoqi Feng. “Natural Depletion
    of Histone H1 in Sex Cells Causes DNA Demethylation, Heterochromatin Decondensation
    and Transposon Activation.” <i>ELife</i>. eLife Sciences Publications, 2019. <a
    href="https://doi.org/10.7554/elife.42530">https://doi.org/10.7554/elife.42530</a>.
  ieee: S. He, M. Vickers, J. Zhang, and X. Feng, “Natural depletion of histone H1
    in sex cells causes DNA demethylation, heterochromatin decondensation and transposon
    activation,” <i>eLife</i>, vol. 8. eLife Sciences Publications, 2019.
  ista: He S, Vickers M, Zhang J, Feng X. 2019. Natural depletion of histone H1 in
    sex cells causes DNA demethylation, heterochromatin decondensation and transposon
    activation. eLife. 8, 42530.
  mla: He, Shengbo, et al. “Natural Depletion of Histone H1 in Sex Cells Causes DNA
    Demethylation, Heterochromatin Decondensation and Transposon Activation.” <i>ELife</i>,
    vol. 8, 42530, eLife Sciences Publications, 2019, doi:<a href="https://doi.org/10.7554/elife.42530">10.7554/elife.42530</a>.
  short: S. He, M. Vickers, J. Zhang, X. Feng, ELife 8 (2019).
date_created: 2023-01-16T09:17:21Z
date_published: 2019-05-28T00:00:00Z
date_updated: 2025-01-14T14:31:41Z
day: '28'
ddc:
- '580'
department:
- _id: XiFe
doi: 10.7554/elife.42530
extern: '1'
external_id:
  unknown:
  - '31135340'
file:
- access_level: open_access
  checksum: ea6b89c20d59e5eb3646916fe5d568ad
  content_type: application/pdf
  creator: alisjak
  date_created: 2023-02-07T09:42:46Z
  date_updated: 2023-02-07T09:42:46Z
  file_id: '12525'
  file_name: 2019_elife_He.pdf
  file_size: 2493837
  relation: main_file
  success: 1
file_date_updated: 2023-02-07T09:42:46Z
fulldoi: https://doi.org/10.7554/elife.42530
has_accepted_license: '1'
intvolume: '         8'
keyword:
- General Immunology and Microbiology
- General Biochemistry
- Genetics and Molecular Biology
- General Medicine
- General Neuroscience
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
publication: eLife
publication_identifier:
  issn:
  - 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Natural depletion of histone H1 in sex cells causes DNA demethylation, heterochromatin
  decondensation and transposon activation
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: 8
year: '2019'
...
---
_id: '15154'
abstract:
- lang: eng
  text: Biofilm formation is critical for the infection cycle of Vibrio cholerae.
    Vibrio exopolysaccharides (VPS) and the matrix proteins RbmA, Bap1 and RbmC are
    required for the development of biofilm architecture. We demonstrate that RbmA
    binds VPS directly and uses a binary structural switch within its first fibronectin
    type III (FnIII-1) domain to control RbmA structural dynamics and the formation
    of VPS-dependent higher-order structures. The structural switch in FnIII-1 regulates
    interactions in trans with the FnIII-2 domain, leading to open (monomeric) or
    closed (dimeric) interfaces. The ability of RbmA to switch between open and closed
    states is important for V. cholerae biofilm formation, as RbmA variants with switches
    that are locked in either of the two states lead to biofilms with altered architecture
    and structural integrity.
article_number: '26163'
article_processing_charge: Yes
article_type: original
author:
- first_name: Jiunn CN
  full_name: Fong, Jiunn CN
  last_name: Fong
- first_name: Andrew
  full_name: Rogers, Andrew
  last_name: Rogers
- first_name: Alicia Kathleen
  full_name: Michael, Alicia Kathleen
  id: 6437c950-2a03-11ee-914d-d6476dd7b75c
  last_name: Michael
- first_name: Nicole C
  full_name: Parsley, Nicole C
  last_name: Parsley
- first_name: William-Cole
  full_name: Cornell, William-Cole
  last_name: Cornell
- first_name: Yu-Cheng
  full_name: Lin, Yu-Cheng
  last_name: Lin
- first_name: Praveen K
  full_name: Singh, Praveen K
  last_name: Singh
- first_name: Raimo
  full_name: Hartmann, Raimo
  last_name: Hartmann
- first_name: Knut
  full_name: Drescher, Knut
  last_name: Drescher
- first_name: Evgeny
  full_name: Vinogradov, Evgeny
  last_name: Vinogradov
- first_name: Lars EP
  full_name: Dietrich, Lars EP
  last_name: Dietrich
- first_name: Carrie L
  full_name: Partch, Carrie L
  last_name: Partch
- first_name: Fitnat H
  full_name: Yildiz, Fitnat H
  last_name: Yildiz
citation:
  ama: Fong JC, Rogers A, Michael AK, et al. Structural dynamics of RbmA governs plasticity
    of Vibrio cholerae biofilms. <i>eLife</i>. 2017;6. doi:<a href="https://doi.org/10.7554/elife.26163">10.7554/elife.26163</a>
  apa: Fong, J. C., Rogers, A., Michael, A. K., Parsley, N. C., Cornell, W.-C., Lin,
    Y.-C., … Yildiz, F. H. (2017). Structural dynamics of RbmA governs plasticity
    of Vibrio cholerae biofilms. <i>ELife</i>. eLife Sciences Publications. <a href="https://doi.org/10.7554/elife.26163">https://doi.org/10.7554/elife.26163</a>
  chicago: Fong, Jiunn CN, Andrew Rogers, Alicia K. Michael, Nicole C Parsley, William-Cole
    Cornell, Yu-Cheng Lin, Praveen K Singh, et al. “Structural Dynamics of RbmA Governs
    Plasticity of Vibrio Cholerae Biofilms.” <i>ELife</i>. eLife Sciences Publications,
    2017. <a href="https://doi.org/10.7554/elife.26163">https://doi.org/10.7554/elife.26163</a>.
  ieee: J. C. Fong <i>et al.</i>, “Structural dynamics of RbmA governs plasticity
    of Vibrio cholerae biofilms,” <i>eLife</i>, vol. 6. eLife Sciences Publications,
    2017.
  ista: Fong JC, Rogers A, Michael AK, Parsley NC, Cornell W-C, Lin Y-C, Singh PK,
    Hartmann R, Drescher K, Vinogradov E, Dietrich LE, Partch CL, Yildiz FH. 2017.
    Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms. eLife.
    6, 26163.
  mla: Fong, Jiunn CN, et al. “Structural Dynamics of RbmA Governs Plasticity of Vibrio
    Cholerae Biofilms.” <i>ELife</i>, vol. 6, 26163, eLife Sciences Publications,
    2017, doi:<a href="https://doi.org/10.7554/elife.26163">10.7554/elife.26163</a>.
  short: J.C. Fong, A. Rogers, A.K. Michael, N.C. Parsley, W.-C. Cornell, Y.-C. Lin,
    P.K. Singh, R. Hartmann, K. Drescher, E. Vinogradov, L.E. Dietrich, C.L. Partch,
    F.H. Yildiz, ELife 6 (2017).
date_created: 2024-03-21T07:55:36Z
date_published: 2017-08-01T00:00:00Z
date_updated: 2024-03-25T12:22:54Z
day: '01'
doi: 10.7554/elife.26163
extern: '1'
external_id:
  pmid:
  - '28762945'
fulldoi: https://doi.org/10.7554/elife.26163
intvolume: '         6'
keyword:
- General Immunology and Microbiology
- General Biochemistry
- Genetics and Molecular Biology
- General Medicine
- General Neuroscience
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.7554/eLife.26163
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: eLife
publication_identifier:
  issn:
  - 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 6
year: '2017'
...
---
_id: '10370'
abstract:
- lang: eng
  text: Eukaryotic cells are densely packed with macromolecular complexes and intertwining
    organelles, continually transported and reshaped. Intriguingly, organelles avoid
    clashing and entangling with each other in such limited space. Mitochondria form
    extensive networks constantly remodeled by fission and fusion. Here, we show that
    mitochondrial fission is triggered by mechanical forces. Mechano-stimulation of
    mitochondria – via encounter with motile intracellular pathogens, via external
    pressure applied by an atomic force microscope, or via cell migration across uneven
    microsurfaces – results in the recruitment of the mitochondrial fission machinery,
    and subsequent division. We propose that MFF, owing to affinity for narrow mitochondria,
    acts as a membrane-bound force sensor to recruit the fission machinery to mechanically
    strained sites. Thus, mitochondria adapt to the environment by sensing and responding
    to biomechanical cues. Our findings that mechanical triggers can be coupled to
    biochemical responses in membrane dynamics may explain how organelles orderly
    cohabit in the crowded cytoplasm.
article_number: e30292
article_processing_charge: No
article_type: original
author:
- first_name: Sebastian Carsten Johannes
  full_name: Helle, Sebastian Carsten Johannes
  last_name: Helle
- first_name: Qian
  full_name: Feng, Qian
  last_name: Feng
- first_name: Mathias J
  full_name: Aebersold, Mathias J
  last_name: Aebersold
- first_name: Luca
  full_name: Hirt, Luca
  last_name: Hirt
- first_name: Raphael R
  full_name: Grüter, Raphael R
  last_name: Grüter
- first_name: Afshin
  full_name: Vahid, Afshin
  last_name: Vahid
- first_name: Andrea
  full_name: Sirianni, Andrea
  last_name: Sirianni
- first_name: Serge
  full_name: Mostowy, Serge
  last_name: Mostowy
- first_name: Jess G
  full_name: Snedeker, Jess G
  last_name: Snedeker
- first_name: Anđela
  full_name: Šarić, Anđela
  id: bf63d406-f056-11eb-b41d-f263a6566d8b
  last_name: Šarić
  orcid: 0000-0002-7854-2139
- first_name: Timon
  full_name: Idema, Timon
  last_name: Idema
- first_name: Tomaso
  full_name: Zambelli, Tomaso
  last_name: Zambelli
- first_name: Benoît
  full_name: Kornmann, Benoît
  last_name: Kornmann
citation:
  ama: Helle SCJ, Feng Q, Aebersold MJ, et al. Mechanical force induces mitochondrial
    fission. <i>eLife</i>. 2017;6. doi:<a href="https://doi.org/10.7554/elife.30292">10.7554/elife.30292</a>
  apa: Helle, S. C. J., Feng, Q., Aebersold, M. J., Hirt, L., Grüter, R. R., Vahid,
    A., … Kornmann, B. (2017). Mechanical force induces mitochondrial fission. <i>ELife</i>.
    eLife Sciences Publications. <a href="https://doi.org/10.7554/elife.30292">https://doi.org/10.7554/elife.30292</a>
  chicago: Helle, Sebastian Carsten Johannes, Qian Feng, Mathias J Aebersold, Luca
    Hirt, Raphael R Grüter, Afshin Vahid, Andrea Sirianni, et al. “Mechanical Force
    Induces Mitochondrial Fission.” <i>ELife</i>. eLife Sciences Publications, 2017.
    <a href="https://doi.org/10.7554/elife.30292">https://doi.org/10.7554/elife.30292</a>.
  ieee: S. C. J. Helle <i>et al.</i>, “Mechanical force induces mitochondrial fission,”
    <i>eLife</i>, vol. 6. eLife Sciences Publications, 2017.
  ista: Helle SCJ, Feng Q, Aebersold MJ, Hirt L, Grüter RR, Vahid A, Sirianni A, Mostowy
    S, Snedeker JG, Šarić A, Idema T, Zambelli T, Kornmann B. 2017. Mechanical force
    induces mitochondrial fission. eLife. 6, e30292.
  mla: Helle, Sebastian Carsten Johannes, et al. “Mechanical Force Induces Mitochondrial
    Fission.” <i>ELife</i>, vol. 6, e30292, eLife Sciences Publications, 2017, doi:<a
    href="https://doi.org/10.7554/elife.30292">10.7554/elife.30292</a>.
  short: S.C.J. Helle, Q. Feng, M.J. Aebersold, L. Hirt, R.R. Grüter, A. Vahid, A.
    Sirianni, S. Mostowy, J.G. Snedeker, A. Šarić, T. Idema, T. Zambelli, B. Kornmann,
    ELife 6 (2017).
date_created: 2021-11-29T08:51:38Z
date_published: 2017-11-09T00:00:00Z
date_updated: 2021-11-29T09:28:14Z
day: '09'
ddc:
- '572'
doi: 10.7554/elife.30292
extern: '1'
external_id:
  pmid:
  - '29119945'
file:
- access_level: open_access
  checksum: c35f42dcfb007f6d6c761a27e24c26d3
  content_type: application/pdf
  creator: cchlebak
  date_created: 2021-11-29T09:07:41Z
  date_updated: 2021-11-29T09:07:41Z
  file_id: '10372'
  file_name: 2017_eLife_Helle.pdf
  file_size: 6120157
  relation: main_file
  success: 1
file_date_updated: 2021-11-29T09:07:41Z
fulldoi: https://doi.org/10.7554/elife.30292
has_accepted_license: '1'
intvolume: '         6'
keyword:
- general immunology and microbiology
- general biochemistry
- genetics and molecular biology
- general medicine
- general neuroscience
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://elifesciences.org/articles/30292
month: '11'
oa: 1
oa_version: Published Version
pmid: 1
publication: eLife
publication_identifier:
  issn:
  - 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mechanical force induces mitochondrial fission
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: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 6
year: '2017'
...