---
_id: '15153'
abstract:
- lang: eng
text: Mammalian circadian rhythms are generated by a transcription-based feedback
loop in which CLOCK:BMAL1 drives transcription of its repressors (PER1/2, CRY1/2),
which ultimately interact with CLOCK:BMAL1 to close the feedback loop with ~24
hr periodicity. Here we pinpoint a key difference between CRY1 and CRY2 that underlies
their differential strengths as transcriptional repressors. Both cryptochromes
bind the BMAL1 transactivation domain similarly to sequester it from coactivators
and repress CLOCK:BMAL1 activity. However, we find that CRY1 is recruited with
much higher affinity to the PAS domain core of CLOCK:BMAL1, allowing it to serve
as a stronger repressor that lengthens circadian period. We discovered a dynamic
serine-rich loop adjacent to the secondary pocket in the photolyase homology region
(PHR) domain that regulates differential binding of cryptochromes to the PAS domain
core of CLOCK:BMAL1. Notably, binding of the co-repressor PER2 remodels the serine
loop of CRY2, making it more CRY1-like and enhancing its affinity for CLOCK:BMAL1.
article_number: '55275'
article_processing_charge: No
article_type: original
author:
- first_name: Jennifer L
full_name: Fribourgh, Jennifer L
last_name: Fribourgh
- first_name: Ashutosh
full_name: Srivastava, Ashutosh
last_name: Srivastava
- first_name: Colby R
full_name: Sandate, Colby R
last_name: Sandate
- first_name: Alicia Kathleen
full_name: Michael, Alicia Kathleen
id: 6437c950-2a03-11ee-914d-d6476dd7b75c
last_name: Michael
- first_name: Peter L
full_name: Hsu, Peter L
last_name: Hsu
- first_name: Christin
full_name: Rakers, Christin
last_name: Rakers
- first_name: Leslee T
full_name: Nguyen, Leslee T
last_name: Nguyen
- first_name: Megan R
full_name: Torgrimson, Megan R
last_name: Torgrimson
- first_name: Gian Carlo G
full_name: Parico, Gian Carlo G
last_name: Parico
- first_name: Sarvind
full_name: Tripathi, Sarvind
last_name: Tripathi
- first_name: Ning
full_name: Zheng, Ning
last_name: Zheng
- first_name: Gabriel C
full_name: Lander, Gabriel C
last_name: Lander
- first_name: Tsuyoshi
full_name: Hirota, Tsuyoshi
last_name: Hirota
- first_name: Florence
full_name: Tama, Florence
last_name: Tama
- first_name: Carrie L
full_name: Partch, Carrie L
last_name: Partch
citation:
ama: Fribourgh JL, Srivastava A, Sandate CR, et al. Dynamics at the serine loop
underlie differential affinity of cryptochromes for CLOCK:BMAL1 to control circadian
timing. eLife. 2020;9. doi:10.7554/elife.55275
apa: Fribourgh, J. L., Srivastava, A., Sandate, C. R., Michael, A. K., Hsu, P. L.,
Rakers, C., … Partch, C. L. (2020). Dynamics at the serine loop underlie differential
affinity of cryptochromes for CLOCK:BMAL1 to control circadian timing. ELife.
eLife Sciences Publications. https://doi.org/10.7554/elife.55275
chicago: Fribourgh, Jennifer L, Ashutosh Srivastava, Colby R Sandate, Alicia K.
Michael, Peter L Hsu, Christin Rakers, Leslee T Nguyen, et al. “Dynamics at the
Serine Loop Underlie Differential Affinity of Cryptochromes for CLOCK:BMAL1 to
Control Circadian Timing.” ELife. eLife Sciences Publications, 2020. https://doi.org/10.7554/elife.55275.
ieee: J. L. Fribourgh et al., “Dynamics at the serine loop underlie differential
affinity of cryptochromes for CLOCK:BMAL1 to control circadian timing,” eLife,
vol. 9. eLife Sciences Publications, 2020.
ista: Fribourgh JL, Srivastava A, Sandate CR, Michael AK, Hsu PL, Rakers C, Nguyen
LT, Torgrimson MR, Parico GCG, Tripathi S, Zheng N, Lander GC, Hirota T, Tama
F, Partch CL. 2020. Dynamics at the serine loop underlie differential affinity
of cryptochromes for CLOCK:BMAL1 to control circadian timing. eLife. 9, 55275.
mla: Fribourgh, Jennifer L., et al. “Dynamics at the Serine Loop Underlie Differential
Affinity of Cryptochromes for CLOCK:BMAL1 to Control Circadian Timing.” ELife,
vol. 9, 55275, eLife Sciences Publications, 2020, doi:10.7554/elife.55275.
short: J.L. Fribourgh, A. Srivastava, C.R. Sandate, A.K. Michael, P.L. Hsu, C. Rakers,
L.T. Nguyen, M.R. Torgrimson, G.C.G. Parico, S. Tripathi, N. Zheng, G.C. Lander,
T. Hirota, F. Tama, C.L. Partch, ELife 9 (2020).
date_created: 2024-03-21T07:55:12Z
date_published: 2020-02-26T00:00:00Z
date_updated: 2024-03-25T12:25:02Z
day: '26'
doi: 10.7554/elife.55275
extern: '1'
fulldoi: https://doi.org/10.7554/elife.55275
intvolume: ' 9'
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.55275
month: '02'
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: Dynamics at the serine loop underlie differential affinity of cryptochromes
for CLOCK:BMAL1 to control circadian timing
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2020'
...
---
_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. eLife. 2019;8. doi:10.7554/elife.49796
apa: 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. eLife Sciences Publications. https://doi.org/10.7554/elife.49796
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.” ELife. eLife Sciences Publications,
2019. https://doi.org/10.7554/elife.49796.
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,” eLife, 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.” ELife, vol. 8,
e49796, eLife Sciences Publications, 2019, doi:10.7554/elife.49796.
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
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.
eLife. 2019;8. doi:10.7554/elife.42530
apa: 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. eLife Sciences Publications. https://doi.org/10.7554/elife.42530
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.” ELife. eLife Sciences Publications, 2019. https://doi.org/10.7554/elife.42530.
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,” eLife, 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.” ELife,
vol. 8, 42530, eLife Sciences Publications, 2019, doi:10.7554/elife.42530.
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: '14286'
abstract:
- lang: eng
text: 'The bacteriophage M13 has found frequent applications in nanobiotechnology
due to its chemically and genetically tunable protein surface and its ability
to self-assemble into colloidal membranes. Additionally, its single-stranded (ss)
genome is commonly used as scaffold for DNA origami. Despite the manifold uses
of M13, upstream production methods for phage and scaffold ssDNA are underexamined
with respect to future industrial usage. Here, the high-cell-density phage production
with Escherichia coli as host organism was studied in respect of medium composition,
infection time, multiplicity of infection, and specific growth rate. The specific
growth rate and the multiplicity of infection were identified as the crucial state
variables that influence phage amplification rate on one hand and the concentration
of produced ssDNA on the other hand. Using a growth rate of 0.15 h−1 and a multiplicity
of infection of 0.05 pfu cfu−1 in the fed-batch production process, the concentration
of pure isolated M13 ssDNA usable for scaffolded DNA origami could be enhanced
by 54% to 590 mg L−1. Thus, our results help enabling M13 production for industrial
uses in nanobiotechnology. Biotechnol. Bioeng. 2017;114: 777–784.'
article_processing_charge: No
article_type: original
author:
- first_name: Benjamin
full_name: Kick, Benjamin
last_name: Kick
- first_name: Samantha
full_name: Hensler, Samantha
last_name: Hensler
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
- first_name: Dirk
full_name: Weuster-Botz, Dirk
last_name: Weuster-Botz
citation:
ama: Kick B, Hensler S, Praetorius FM, Dietz H, Weuster-Botz D. Specific growth
rate and multiplicity of infection affect high-cell-density fermentation with
bacteriophage M13 for ssDNA production. Biotechnology and Bioengineering.
2017;114(4):777-784. doi:10.1002/bit.26200
apa: Kick, B., Hensler, S., Praetorius, F. M., Dietz, H., & Weuster-Botz, D.
(2017). Specific growth rate and multiplicity of infection affect high-cell-density
fermentation with bacteriophage M13 for ssDNA production. Biotechnology and
Bioengineering. Wiley. https://doi.org/10.1002/bit.26200
chicago: Kick, Benjamin, Samantha Hensler, Florian M Praetorius, Hendrik Dietz,
and Dirk Weuster-Botz. “Specific Growth Rate and Multiplicity of Infection Affect
High-Cell-Density Fermentation with Bacteriophage M13 for SsDNA Production.” Biotechnology
and Bioengineering. Wiley, 2017. https://doi.org/10.1002/bit.26200.
ieee: B. Kick, S. Hensler, F. M. Praetorius, H. Dietz, and D. Weuster-Botz, “Specific
growth rate and multiplicity of infection affect high-cell-density fermentation
with bacteriophage M13 for ssDNA production,” Biotechnology and Bioengineering,
vol. 114, no. 4. Wiley, pp. 777–784, 2017.
ista: Kick B, Hensler S, Praetorius FM, Dietz H, Weuster-Botz D. 2017. Specific
growth rate and multiplicity of infection affect high-cell-density fermentation
with bacteriophage M13 for ssDNA production. Biotechnology and Bioengineering.
114(4), 777–784.
mla: Kick, Benjamin, et al. “Specific Growth Rate and Multiplicity of Infection
Affect High-Cell-Density Fermentation with Bacteriophage M13 for SsDNA Production.”
Biotechnology and Bioengineering, vol. 114, no. 4, Wiley, 2017, pp. 777–84,
doi:10.1002/bit.26200.
short: B. Kick, S. Hensler, F.M. Praetorius, H. Dietz, D. Weuster-Botz, Biotechnology
and Bioengineering 114 (2017) 777–784.
date_created: 2023-09-06T12:08:29Z
date_published: 2017-04-01T00:00:00Z
date_updated: 2023-11-07T12:36:20Z
day: '01'
doi: 10.1002/bit.26200
extern: '1'
external_id:
pmid:
- '27748519'
fulldoi: https://doi.org/10.1002/bit.26200
intvolume: ' 114'
issue: '4'
keyword:
- Applied Microbiology and Biotechnology
- Bioengineering
- Biotechnology
language:
- iso: eng
month: '04'
oa_version: None
page: 777-784
pmid: 1
publication: Biotechnology and Bioengineering
publication_identifier:
issn:
- 0006-3592
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Specific growth rate and multiplicity of infection affect high-cell-density
fermentation with bacteriophage M13 for ssDNA production
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 114
year: '2017'
...
---
_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. eLife. 2017;6. doi:10.7554/elife.26163
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. ELife. eLife Sciences Publications. https://doi.org/10.7554/elife.26163
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.” ELife. eLife Sciences Publications,
2017. https://doi.org/10.7554/elife.26163.
ieee: J. C. Fong et al., “Structural dynamics of RbmA governs plasticity
of Vibrio cholerae biofilms,” eLife, 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.” ELife, vol. 6, 26163, eLife Sciences Publications,
2017, doi:10.7554/elife.26163.
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. eLife. 2017;6. doi:10.7554/elife.30292
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. ELife.
eLife Sciences Publications. https://doi.org/10.7554/elife.30292
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.” ELife. eLife Sciences Publications, 2017.
https://doi.org/10.7554/elife.30292.
ieee: S. C. J. Helle et al., “Mechanical force induces mitochondrial fission,”
eLife, 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.” ELife, vol. 6, e30292, eLife Sciences Publications, 2017, doi:10.7554/elife.30292.
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'
...