---
OA_place: publisher
OA_type: hybrid
_id: '22269'
abstract:
- lang: eng
text: The divisome apparatus synthesizes septal peptidoglycan (PG) during bacterial
division. In Escherichia coli, the class A penicillin-binding protein (aPBP) called
PBP1b has been implicated in division, but its role in the process has remained
unclear. Here we show using in situ cryo-electron tomography, genetics and other
imaging methods that PBP1b is required to produce a wedge-like density of PG at
the division site and that loss of this structure weakens the division site, making
it hypersusceptible to osmotic lysis. Surprisingly, the activator LpoB needed
for general PBP1b function was not required for its role in division. Of the two
PBP1b isoforms produced in cells, we show that the one with an extended cytoplasmic
N terminus localizes to and functions at the division site, probably via recruitment
by the FtsA component of the divisome. The conservation of aPBPs with extended
cytoplasmic N termini suggests that other Gram-negative bacteria may use similar
mechanisms for division site reinforcement.
acknowledgement: We thank all members of the Bernhardt, Rudner, Navarro and Vettiger
Laboratories for support and helpful conversations. We thank C. Genoud, J. Daraspe,
A. Mucciolo and D. de Bellis at the Electron Microscopy Facility of the University
of Lausanne and E. Jeanvoine for providing access to workstations for cryo-ET image
processing; S. Sterling, C. Borsa, J. Podgorski, P. Vinh Dip, E. Brignole and A.
Osherov at the MIT.nano cryo-EM facility, K. Song and C. Xu at the University of
Massachusetts cryo-EM facility, and R. Walsh and Z. Li at the cryo-EM at Harvard
Medical School facility for providing access to the cryo-EM microscopes and for
all their help, advice and maintenance of cryo-EM equipment. AFM was performed at
the Harvard University Center for Nanoscale Systems (CNS), a member of the National
Nanotechnology Coordinated Infrastructure Network (NNCI), which is supported by
the National Science Foundation under NSF award no. ECCS-2025158. We thank N. S.
Colella for excellent advice on AFM data acquisition and analysis; the MicRoN imaging
core at Harvard Medical School for excellent advice on live cell imaging and maintenance
of fluorescence microscopes; B. Krautz for creating the cartoon illustrations (www.sciencecommunicated.com);
and L. Miles and R. Aeschimann for assistance with strain construction. A.V. was
supported by an EMBO long-term postdoctoral fellowship ALTF_89-2019, the Swiss National
Science Foundation (SNSF) Postdoc.Mobility fellowship P500PB_203143. P.P.N. was
a recipient of early postdoc.mobility and postdoc.mobility fellowships (P2BSP3_188112
and P400PB_199252). This work was also supported by funding from the National Institutes
of Health (R35GM142553 to L.H.C. and R01AI083365 to T.G.B.), investigator funds
from the Howard Hughes Medical Institute (T.G.B.), an SNSF project grant (320030-236243
to A.V.), an SNSF Starting Grant (TMSGI3_218251 to P.P.N.), an SNSF Project grant
(320030-236069 to P.P.N), an SNSF SPARK grant (CRSK-3_237167 to P.P.N.), cryo-EM
funds from the Faculty of Biology and Medicine at University of Lausanne to P.P.N.
and the Foundation Pierre Mercier pour la Science (to P.P.N.).
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Paula P.
full_name: Navarro, Paula P.
last_name: Navarro
- first_name: Andrea
full_name: Vettiger, Andrea
last_name: Vettiger
- first_name: Roman
full_name: Hajdu, Roman
id: ffab949d-133f-11ed-8f02-94de21ace503
last_name: Hajdu
- first_name: Virly Y.
full_name: Ananda, Virly Y.
last_name: Ananda
- first_name: Alejandro
full_name: López-Tavares, Alejandro
last_name: López-Tavares
- first_name: Ernst W.
full_name: Schmid, Ernst W.
last_name: Schmid
- first_name: Johannes C.
full_name: Walter, Johannes C.
last_name: Walter
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Luke H.
full_name: Chao, Luke H.
last_name: Chao
- first_name: Thomas G.
full_name: Bernhardt, Thomas G.
last_name: Bernhardt
citation:
ama: Navarro PP, Vettiger A, Hajdu R, et al. The penicillin-binding protein PBP1b
fortifies the Escherichia coli division site against osmotic rupture. Nature
Microbiology. 2026. doi:10.1038/s41564-026-02403-6
apa: Navarro, P. P., Vettiger, A., Hajdu, R., Ananda, V. Y., López-Tavares, A.,
Schmid, E. W., … Bernhardt, T. G. (2026). The penicillin-binding protein PBP1b
fortifies the Escherichia coli division site against osmotic rupture. Nature
Microbiology. Springer Nature. https://doi.org/10.1038/s41564-026-02403-6
chicago: Navarro, Paula P., Andrea Vettiger, Roman Hajdu, Virly Y. Ananda, Alejandro
López-Tavares, Ernst W. Schmid, Johannes C. Walter, Martin Loose, Luke H. Chao,
and Thomas G. Bernhardt. “The Penicillin-Binding Protein PBP1b Fortifies the Escherichia
Coli Division Site against Osmotic Rupture.” Nature Microbiology. Springer
Nature, 2026. https://doi.org/10.1038/s41564-026-02403-6.
ieee: P. P. Navarro et al., “The penicillin-binding protein PBP1b fortifies
the Escherichia coli division site against osmotic rupture,” Nature Microbiology.
Springer Nature, 2026.
ista: Navarro PP, Vettiger A, Hajdu R, Ananda VY, López-Tavares A, Schmid EW, Walter
JC, Loose M, Chao LH, Bernhardt TG. 2026. The penicillin-binding protein PBP1b
fortifies the Escherichia coli division site against osmotic rupture. Nature Microbiology.
mla: Navarro, Paula P., et al. “The Penicillin-Binding Protein PBP1b Fortifies the
Escherichia Coli Division Site against Osmotic Rupture.” Nature Microbiology,
Springer Nature, 2026, doi:10.1038/s41564-026-02403-6.
short: P.P. Navarro, A. Vettiger, R. Hajdu, V.Y. Ananda, A. López-Tavares, E.W.
Schmid, J.C. Walter, M. Loose, L.H. Chao, T.G. Bernhardt, Nature Microbiology
(2026).
das_tickbox: '1'
dataavailabilitystatement: 'The data, plasmids and strains that support the findings
of this study are available from the corresponding authors by request. Representative
tomograms are deposited in EMDB: EMD-27479 (wild-type), EMD-53351 (∆ponB), EMD-53357(∆lpoB)
and EMD-53363 (∆ponA). Corresponding raw movie frames and stacks of tilt series
are deposited as EMPIAR-11090 (wild type), EMPIAR-13502 (∆ponB), EMPIAR-13513 (∆lpoB)
and EMPIAR-13512 (∆ponA), and will be released upon publication. Other data related
to this manuscript (for example, AFM, light microscopy, growth curves and so on)
can be found on Zenodo at https://doi.org/10.5281/zenodo.20841819 (ref. 101). Source
data are provided with this paper. Scripts used in this study were deposited on
GitHub at https://github.com/NavarroVettiger/Navarro-et-al_2022 and https://github.com/virlyananda/EM-ImageProcessing.'
date_created: 2026-07-12T22:02:19Z
date_published: 2026-07-03T00:00:00Z
date_updated: 2026-07-13T09:22:49Z
day: '03'
ddc:
- '570'
department:
- _id: MaLo
- _id: GradSch
doi: 10.1038/s41564-026-02403-6
external_id:
pmid:
- '42399561'
fulldoi: https://doi.org/10.1038/s41564-026-02403-6
has_accepted_license: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41564-026-02403-6
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Microbiology
publication_identifier:
eissn:
- 2058-5276
publication_status: epub_ahead
publisher: Springer Nature
quality_controlled: '1'
researchdata_availability: yes
scopus_import: '1'
status: public
supplementarymaterial: yes
title: The penicillin-binding protein PBP1b fortifies the Escherichia coli division
site against osmotic rupture
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
year: '2026'
...
---
OA_place: publisher
OA_type: hybrid
_id: '22647'
abstract:
- lang: eng
text: "Within the plant endomembrane system, the vesicle coat protein clathrin localizes
to the plasma membrane (PM) and the trans-Golgi Network/early endosome (TGN/EE).
While the role of clathrin in endocytosis at the PM is well established, its function
at TGN/EE, presumably in late secretion (trafficking from the TGN/EE to the cell
surface) or en route to the vacuole, is debated. Similarly debated are potential
homeostatic mechanisms balancing the trafficking routes, especially endocytosis
and late secretion.\r\nWe address these questions in Arabidopsis thaliana using
conditional silencing of CLATHRIN HEAVY CHAIN (CHC), conditional overexpression
of the clathrin uncoating factor AUXILIN-LIKE1, and secretory mutants.\r\nCHC
silencing interferes with trafficking of cargoes destined for the apoplast and
the PM, supporting a function of clathrin in late secretion. The secretory cargoes
become abnormally rerouted from the TGN/EE to the vacuole. Unlike CHC silencing,
overexpression of AUXILIN-LIKE1 selectively inhibits clathrin-mediated endocytosis
while secretion continues normally at early points of induction. Conversely, secretory
mutants exhibit a reduced PM recruitment of clathrin, and variably, of the TPLATE
endocytic component.\r\nTogether, our data show a role of clathrin in secretion
and suggest secretion as a fundamental trafficking process to which endocytosis
is adjusted by a weak homeostatic mechanism."
acknowledgement: 'The authors wish to acknowledge Dr. Paweł Baster for cloning PIN1-GFP-2/pDONR221,
Ms. Aline Monzer and Dr. Mingyue Li for help with CHC protein level evaluation,
Dr. Michał Rychłowski for help with confocal microscopy, Prof. Ari Pekka Mähönen
for sharing the p1R4-pUBQ10:XVE plasmid, and Prof. Ying Gu for sharing seeds of
the sec5 mutant. M.A. would like to thank Dr. Xixi Zhang and Prof. Sebastian Bednarek
for inspiring discussions. This work was supported by the Taif University Researchers
Supporting Project, TURSP-HC2022/02 to JF and SA and Austrian Science Fund (FWF):
I 3630-B25 to JF. Open Access funding provided by Institute of Science and Technology
Austria.'
article_number: nph.71454
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Maciek
full_name: Adamowski, Maciek
id: 45F536D2-F248-11E8-B48F-1D18A9856A87
last_name: Adamowski
orcid: 0000-0001-6463-5257
- first_name: Adam
full_name: Gackowski, Adam
last_name: Gackowski
- first_name: Ivana
full_name: Matijevic, Ivana
id: 83c17ce3-15b2-11ec-abd3-f486545870bd
last_name: Matijevic
- first_name: Saqer S.
full_name: Alotaibi, Saqer S.
last_name: Alotaibi
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Adamowski M, Gackowski A, Matijevic I, Alotaibi SS, Friml J. The role of clathrin
in post‐Golgi secretion in plant cells. New Phytologist. 2026. doi:10.1111/nph.71454
apa: Adamowski, M., Gackowski, A., Matijevic, I., Alotaibi, S. S., & Friml,
J. (2026). The role of clathrin in post‐Golgi secretion in plant cells. New
Phytologist. Wiley. https://doi.org/10.1111/nph.71454
chicago: Adamowski, Maciek, Adam Gackowski, Ivana Matijevic, Saqer S. Alotaibi,
and Jiří Friml. “The Role of Clathrin in Post‐Golgi Secretion in Plant Cells.”
New Phytologist. Wiley, 2026. https://doi.org/10.1111/nph.71454.
ieee: M. Adamowski, A. Gackowski, I. Matijevic, S. S. Alotaibi, and J. Friml, “The
role of clathrin in post‐Golgi secretion in plant cells,” New Phytologist.
Wiley, 2026.
ista: Adamowski M, Gackowski A, Matijevic I, Alotaibi SS, Friml J. 2026. The role
of clathrin in post‐Golgi secretion in plant cells. New Phytologist., nph. 71454.
mla: Adamowski, Maciek, et al. “The Role of Clathrin in Post‐Golgi Secretion in
Plant Cells.” New Phytologist, nph. 71454, Wiley, 2026, doi:10.1111/nph.71454.
short: M. Adamowski, A. Gackowski, I. Matijevic, S.S. Alotaibi, J. Friml, New Phytologist
(2026).
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: 'Original data associated with this study have been deposited
in Dataset S1. The accession nos. of A. thaliana genes used in this study are as
follows: CHC1 (AT3G11130), CHC2 (AT3G08530), CLC2 (AT2G40060), TPLATE (AT3G01780),
AP2A1 (AT5G22770), DRP1C (AT1G14830), GNOM-LIKE1 (AT5G39500), BEN3/BIG2 (AT3G60860),
TMK4 (AT3G23750), PIN1 (AT1G73590), AUXILIN-LIKE1 (AT4G12780), AP1M2 (AT1G60780),
ECHIDNA (AT1G09330), SEC5A (AT1G76850), SEC5B (AT1G21170), TUB2 (AT5G62690), and
PP2AA3 (AT1G13320).'
date_created: 2026-08-04T06:48:41Z
date_published: 2026-07-20T00:00:00Z
date_updated: 2026-08-04T07:58:27Z
day: '20'
department:
- _id: JiFr
- _id: MaLo
- _id: GradSch
doi: 10.1111/nph.71454
external_id:
pmid:
- '42477503'
fulldoi: https://doi.org/10.1111/nph.71454
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1111/nph.71454
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
publication: New Phytologist
publication_identifier:
eissn:
- 1469-8137
issn:
- 0028-646X
publication_status: epub_ahead
publisher: Wiley
quality_controlled: '1'
researchdata_availability: yes
scopus_import: '1'
status: public
supplementarymaterial: yes
title: The role of clathrin in post‐Golgi secretion in plant cells
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2026'
...
---
OA_type: closed access
_id: '21762'
abstract:
- lang: eng
text: Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular
organization. The plasmid-encoded ParMRC system forms actin-like filaments that
segregate low–copy number plasmids. In multicellular cyanobacteria such as Anabaena
sp., we found that a chromosomally encoded ParMR system has evolved into a cytoskeletal
system named CorMR with a function in cell shape control rather than DNA segregation.
Live-cell imaging, in vitro reconstitution, and cryo–electron microscopy revealed
that CorM formed dynamically unstable, antiparallel double-stranded filaments
that were recruited to the membrane by CorR through an amphipathic helix conserved
in multicellular cyanobacteria. CorMR filaments were regulated by MinC, which
excluded them from the poles and division plane. Comparative genomics indicated
that the repurposing of ParMR and Min systems coevolved with cyanobacterial multicellularity,
highlighting the evolutionary plasticity of cytoskeletal systems in bacteria.
acknowledged_ssus:
- _id: Bio
- _id: ScienComp
- _id: EM-Fac
- _id: LifeSc
acknowledgement: "We thank all members of the Loose lab at ISTA for helpful discussions;
M. Kojic for critical reading of the manuscript; A. Herrero (Sevilla University)
for sharing her extensive BACTH plasmid library and other plasmids, as well as cyanobacterial
strains; T. Dagan and F. Nies (both Kiel University) for sharing cyanobacterial
strains and plasmids and for valuable discussions; N. Sapay and A. Michon for providing
the Amphipaseek code, which enabled us to perform our large-scale amphipathic helix
screen of cyanobacterial CorR proteins; V.-V. Hodirnau for support in cryo-ET data
collection; and J. Hansen for advice about cryo-EM data processing.\r\nThis work
was supported by the Scientific Service Units (SSU) of ISTA through resources provided
by the Imaging & Optics Facility (IOF), the Scientific Computing (SciComp), the
Electron Microscopy Facility (EMF), and the Lab Support Facility (LSF). This work
was funded by the European Union’s Horizon 2020 research and innovation program
(Marie Skłodowska-Curie grant 101034413 to B.L.S.); the European Research Council
(ERC) of the European Union (grant ActinID 101076260 to F.K.M.S.); the Swiss National
Science Foundation (starting grant TMSGI3_226208 to G.L.W.); and the Jean-Jacques
et Letitia Lopez-Loreta Foundation (G.L.W.)."
article_number: eaea6343
article_processing_charge: No
article_type: original
author:
- first_name: Benjamin L
full_name: Springstein, Benjamin L
id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083
last_name: Springstein
orcid: 0000-0002-3461-5391
- first_name: Manjunath
full_name: Javoor, Manjunath
id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2
last_name: Javoor
orcid: 0000-0003-2311-2112
- first_name: Daniela
full_name: Megrian, Daniela
last_name: Megrian
- first_name: Roman
full_name: Hajdu, Roman
id: ffab949d-133f-11ed-8f02-94de21ace503
last_name: Hajdu
- first_name: Dustin M.
full_name: Hanke, Dustin M.
last_name: Hanke
- first_name: Bettina
full_name: Zens, Bettina
id: 45FD126C-F248-11E8-B48F-1D18A9856A87
last_name: Zens
orcid: 0000-0002-9561-1239
- first_name: Gregor L.
full_name: Weiss, Gregor L.
last_name: Weiss
- first_name: Florian Km
full_name: Schur, Florian Km
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Springstein BL, Javoor M, Megrian D, et al. Repurposing of a DNA segregation
machinery into a cytoskeletal system controlling cell shape. Science. 2026;392(6795).
doi:10.1126/science.aea6343
apa: Springstein, B. L., Javoor, M., Megrian, D., Hajdu, R., Hanke, D. M., Zens,
B., … Loose, M. (2026). Repurposing of a DNA segregation machinery into a cytoskeletal
system controlling cell shape. Science. AAAS. https://doi.org/10.1126/science.aea6343
chicago: Springstein, Benjamin L, Manjunath Javoor, Daniela Megrian, Roman Hajdu,
Dustin M. Hanke, Bettina Zens, Gregor L. Weiss, Florian KM Schur, and Martin Loose.
“Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling
Cell Shape.” Science. AAAS, 2026. https://doi.org/10.1126/science.aea6343.
ieee: B. L. Springstein et al., “Repurposing of a DNA segregation machinery
into a cytoskeletal system controlling cell shape,” Science, vol. 392,
no. 6795. AAAS, 2026.
ista: Springstein BL, Javoor M, Megrian D, Hajdu R, Hanke DM, Zens B, Weiss GL,
Schur FK, Loose M. 2026. Repurposing of a DNA segregation machinery into a cytoskeletal
system controlling cell shape. Science. 392(6795), eaea6343.
mla: Springstein, Benjamin L., et al. “Repurposing of a DNA Segregation Machinery
into a Cytoskeletal System Controlling Cell Shape.” Science, vol. 392,
no. 6795, eaea6343, AAAS, 2026, doi:10.1126/science.aea6343.
short: B.L. Springstein, M. Javoor, D. Megrian, R. Hajdu, D.M. Hanke, B. Zens, G.L.
Weiss, F.K. Schur, M. Loose, Science 392 (2026).
corr_author: '1'
date_created: 2026-04-26T22:01:46Z
date_published: 2026-04-16T00:00:00Z
date_updated: 2026-09-03T09:36:24Z
day: '16'
department:
- _id: MaLo
- _id: FlSc
- _id: GradSch
- _id: EM-Fac
doi: 10.1126/science.aea6343
ec_funded: 1
external_id:
pmid:
- '41990175'
fulldoi: https://doi.org/10.1126/science.aea6343
intvolume: ' 392'
issue: '6795'
language:
- iso: eng
month: '04'
oa_version: None
pmid: 1
project:
- _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c
call_identifier: H2020
grant_number: '101034413'
name: 'IST-BRIDGE: International postdoctoral program'
- _id: bd980d18-d553-11ed-ba76-ceaa645c97eb
grant_number: '101076260'
name: A molecular atlas of Actin filament IDentities in the cell motility machinery
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: AAAS
quality_controlled: '1'
related_material:
record:
- id: '22744'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Repurposing of a DNA segregation machinery into a cytoskeletal system controlling
cell shape
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 392
year: '2026'
...
---
_id: '19915'
acknowledgement: "We thank all members of the Martin Loose lab at ISTA for helpful
discussions and Marko Kojic for critical reading of the manuscript. This research
was supported by the Scientific Service Units (SSU) of ISTA through resources provided
by the Imaging & Optics Facility (IOF), the Scientific Computing (SciComp) and the
Electron Microscopy Facility (EMF), as well as the Lab Support Facility (LSF). This
project has received funding from the European Union’s Horizon 2020 research and
innovation program under the Marie Skłodowska-Curie Grant Agreement No.101034413
awarded to BLS as well as an ERC grant (ActinID, 101076260) from the European Union
awarded to FKMS. Views and opinions expressed are however those of the author(s)
only and do not necessarily reflect those of the European Union or the European
Research Council. Neither the European Union nor the granting authority can be held
responsible for them.\r\n\r\nWe are grateful for Antonia Herrero (Sevilla University)
for sharing her extensive BACTH plasmid library and other plasmids as well as cyanobacterial
strains. Likewise, we would like to thank Tal Dagan and Fabian Nies (both Kiel University)
for sharing cyanobacterial strains and plasmids and for valuable discussions.\r\n\r\nWe
would further like to express our gratitude to Nicolas Sapay and Alexis Michon for
providing the Amphipaseek code, which enabled us to perform our large-scale amphipathic
helix screen of cyanobacterial CorR proteins. Finally, we also want to thank Jesse
Hansen for advice in cryo-EM data processing"
article_processing_charge: No
author:
- first_name: Benjamin L
full_name: Springstein, Benjamin L
id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083
last_name: Springstein
orcid: 0000-0002-3461-5391
citation:
ama: Springstein BL. Files for “Evolutionary repurposing of a DNA segregation machinery
into a cytoskeletal system controlling cyanobacterial cell shape.” 2025. doi:10.15479/AT:ISTA:19915
apa: Springstein, B. L. (2025). Files for “Evolutionary repurposing of a DNA segregation
machinery into a cytoskeletal system controlling cyanobacterial cell shape.” Institute
of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:19915
chicago: Springstein, Benjamin L. “Files for ‘Evolutionary Repurposing of a DNA
Segregation Machinery into a Cytoskeletal System Controlling Cyanobacterial Cell
Shape.’” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT:ISTA:19915.
ieee: B. L. Springstein, “Files for ‘Evolutionary repurposing of a DNA segregation
machinery into a cytoskeletal system controlling cyanobacterial cell shape.’”
Institute of Science and Technology Austria, 2025.
ista: Springstein BL. 2025. Files for ‘Evolutionary repurposing of a DNA segregation
machinery into a cytoskeletal system controlling cyanobacterial cell shape’, Institute
of Science and Technology Austria, 10.15479/AT:ISTA:19915.
mla: Springstein, Benjamin L. Files for “Evolutionary Repurposing of a DNA Segregation
Machinery into a Cytoskeletal System Controlling Cyanobacterial Cell Shape.”
Institute of Science and Technology Austria, 2025, doi:10.15479/AT:ISTA:19915.
short: B.L. Springstein, (2025).
contributor:
- contributor_type: project_leader
first_name: Benjamin L
id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083
last_name: Springstein
orcid: 0000-0002-3461-5391
- contributor_type: researcher
first_name: Manjunath
id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2
last_name: Javoor
- contributor_type: researcher
first_name: Daniela
last_name: Megrian
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name: A molecular atlas of Actin filament IDentities in the cell motility machinery
publisher: Institute of Science and Technology Austria
status: public
title: Files for "Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal
system controlling cyanobacterial cell shape"
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abstract:
- lang: eng
text: Rab GTPases organize intracellular trafficking and provide identity to organelles.
Their spatiotemporal activation by guanine nucleotide exchange factors (GEFs)
is tightly controlled to ensure fidelity. Our structural and functional comparison
of the tri-longin domain RabGEFs Mon1-Ccz1 and Fuzzy-Inturned reveals the molecular
basis for their target specificity. Both complexes rely on a conserved sequence
motif of their substrate GTPases for the catalytic mechanism, while secondary
interactions allow discrimination between targets. We also find that dimeric Mon1-Ccz1
from fungi and the metazoan homologs with the additional third subunit RMC1/Bulli
bind membranes through electrostatic interactions via distinct interfaces. Protein-lipid
interaction studies and functional characterization in flies reveal an essential
function of RMC1/Bulli as mediator of GEF complex membrane recruitment. In the
case of Fuzzy-Inturned, reconstitution experiments demonstrate that the BAR (Bin-Amphiphysin-Rvs)
domain protein CiBAR1 can support membrane recruitment of the GEF. Collectively,
our study demonstrates the molecular basis for the adaptation of TLD-RabGEFs to
different cellular functions.
acknowledgement: 'We thank A.-M. Lawrence-Dörner and B. Berkenfeld for technical assistance
and the members of the Kümmel Lab for constructive feedback. We are grateful to
C. Ungermann and L. Langemeyer for insightful discussions and to F. Barr for providing
plasmids encoding Fuzzy, Inturned, Rab23, and Rsg1. The template clone Flag-ciBAR1
was a gift from K.-I. Takemaru (Addgene, plasmid #200440). We thank the Bloomington
Drosophila Stock center (BDSC) and DSHB for providing fly stocks and antibodies.
This work was supported by the German Research Foundation (DFG) through the grants
SFB1557-P10 (D.K.), SFB1557-P11 (A.M.), and SFB1577-P6, PA517/12-2, PA517/14-1,
PA517/15-1, and PA517/16-1 (A.P.). Cryo-EM data were collected at the infrastructure
of the University of Osnabrück, funded by the DFG (project number 455249646). J.-H.S.
was supported by the Friedrich-Ebert Foundation. M.L. acknowledges funding from
the European Research Council (ERC) under the European Union’s Horizon 2020 research
and innovation program (grant agreement number 101045340).'
article_processing_charge: Yes
article_type: original
author:
- first_name: Stephan
full_name: Wilmes, Stephan
last_name: Wilmes
- first_name: Jesse
full_name: Tönjes, Jesse
last_name: Tönjes
- first_name: Maik
full_name: Drechsler, Maik
last_name: Drechsler
- first_name: Anita
full_name: Ruf, Anita
last_name: Ruf
- first_name: Jan Hannes
full_name: Schäfer, Jan Hannes
last_name: Schäfer
- first_name: Anna
full_name: Lürick, Anna
last_name: Lürick
- first_name: Dovile
full_name: Januliene, Dovile
last_name: Januliene
- first_name: Steven
full_name: Apelt, Steven
last_name: Apelt
- first_name: Daniele
full_name: Di Iorio, Daniele
last_name: Di Iorio
- first_name: Seraphine V.
full_name: Wegner, Seraphine V.
last_name: Wegner
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Arne
full_name: Moeller, Arne
last_name: Moeller
- first_name: Achim
full_name: Paululat, Achim
last_name: Paululat
- first_name: Daniel
full_name: Kümmel, Daniel
last_name: Kümmel
citation:
ama: Wilmes S, Tönjes J, Drechsler M, et al. Mechanistic adaptation of the metazoan
RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. Science Advances. 2025;11(35):eadx2893.
doi:10.1126/sciadv.adx2893
apa: Wilmes, S., Tönjes, J., Drechsler, M., Ruf, A., Schäfer, J. H., Lürick, A.,
… Kümmel, D. (2025). Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1
and Fuzzy-Inturned. Science Advances. AAAS. https://doi.org/10.1126/sciadv.adx2893
chicago: Wilmes, Stephan, Jesse Tönjes, Maik Drechsler, Anita Ruf, Jan Hannes Schäfer,
Anna Lürick, Dovile Januliene, et al. “Mechanistic Adaptation of the Metazoan
RabGEFs Mon1-Ccz1 and Fuzzy-Inturned.” Science Advances. AAAS, 2025. https://doi.org/10.1126/sciadv.adx2893.
ieee: S. Wilmes et al., “Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1
and Fuzzy-Inturned,” Science Advances, vol. 11, no. 35. AAAS, p. eadx2893,
2025.
ista: Wilmes S, Tönjes J, Drechsler M, Ruf A, Schäfer JH, Lürick A, Januliene D,
Apelt S, Di Iorio D, Wegner SV, Loose M, Moeller A, Paululat A, Kümmel D. 2025.
Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. Science
Advances. 11(35), eadx2893.
mla: Wilmes, Stephan, et al. “Mechanistic Adaptation of the Metazoan RabGEFs Mon1-Ccz1
and Fuzzy-Inturned.” Science Advances, vol. 11, no. 35, AAAS, 2025, p.
eadx2893, doi:10.1126/sciadv.adx2893.
short: S. Wilmes, J. Tönjes, M. Drechsler, A. Ruf, J.H. Schäfer, A. Lürick, D. Januliene,
S. Apelt, D. Di Iorio, S.V. Wegner, M. Loose, A. Moeller, A. Paululat, D. Kümmel,
Science Advances 11 (2025) eadx2893.
date_created: 2025-09-14T22:01:32Z
date_published: 2025-08-29T00:00:00Z
date_updated: 2025-09-30T14:40:27Z
day: '29'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1126/sciadv.adx2893
external_id:
isi:
- '001559806100033'
pmid:
- '40864718'
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issue: '35'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
page: eadx2893
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project:
- _id: bd6ae2ca-d553-11ed-ba76-a4aa239da5ee
grant_number: '101045340'
name: Synthetic and structural biology of Rab GTPase networks
publication: Science Advances
publication_identifier:
eissn:
- 2375-2548
publication_status: published
publisher: AAAS
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned
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: 11
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...
---
OA_place: publisher
_id: '20741'
abstract:
- lang: eng
text: "Life on Earth emerged when biomacromolecules were membrane-enclosed in a
confined space where many essential chemical reactions were more likely to happen
and thereby accelerate evolution. These kinds of membranes separated internal
reactions from the outside chaos while staying flexible so that those primordial
cells can move, adopt their shape and, most importantly, propagate. Such membrane
plasticity still remains a defining feature of all modern cell types. This remarkable
ability to change their shape is most prominently observed during their propagation
(i.e., cell division). Throughout division, a cell undergoes drastic change in
its shape, usually at the middle of the cell, pulling the two opposite membrane
sides inward, closer to each other, and, finally, culminating in pinching off
to separate the cell into two daughter cells. To achieve this, a cell needs to
employ a protein machinery, usually termed divisome, that can coordinate all necessary
intracellular processes with membrane remodelling and synthesis of other extracellular
structures that decorate a cell. The focus of this dissertation is a membrane-remodelling
FtsZ system that is present across all domains of life. FtsZ forms filaments that
further self-organize into ring-like structures at the cell septum and together
with other division proteins perform cell envelope synthesis and constriction.
However, there are still knowledge gaps in our mechanistic understanding of division
in both archaea and bacteria. My work presented in this dissertation centres around
a simple yet not well understood question: How is the divisome positioned correctly
at the mid-cell? To achieve the proper positioning, the divisome needs to (i)
be recruited to the mid-cell and (ii) localized orthogonally to the long cell
axis. I tackle these processes in two different systems by applying an in vitro
biochemical bottom-up reconstitution approach. I use purified components of Haloferax
volcanii and Escherichia coli divisome to explore how divisome is recruited to
the mid-cell in archaea and how the Z-ring positions orthogonally to the long
cell axis in bacteria, respectively. \r\n\r\nFirstly, I collaborate with archaeal
cell and structural biologists to explore the assembly of early division proteins
in two FtsZ-containing archaeon H. volcanii, a standard model system for understudied
archaeal organisms. I particularly address the hierarchy of interactions that
allow a tripartite complex formation (SepF-CdpB1-CdpB2) and how the hierarchy
of interactions ultimately leads to the recruitment of FtsZ filaments to the septum.
This part of work has been published in (Nußbaum et al., 2024). In collaboration
with evolutionary biologists, I shed light on ancient features that archaeal divisome
has retained to this day and also speculate on a property that it might have lost
during the course of evolution. \r\n\r\nNext, I switch my attention to E. coli
divisome. Particularly, I address the FtsZ’s intrinsic biophysical property that
drives the Z-ring diameter, and thereby the perpendicular orientation of the Z-ring
to the long cell axis based on suggested membrane curvature sensing mechanism
(Vanhille-Campos et al., 2024). This property allows formation of different Z-ring
diameters that match the variety of cell diameters present in prokaryotes. The
results showcase that the distribution of charged amino acids in the intrinsically
disordered linker at the C-terminus (CTL) of FtsZ is the major determining factor
of Z-ring diameter with inter-CTL interactions as an underlying mechanism. \r\n\r\nFinally,
I thoroughly explain the methodology I used to address the abovementioned projects,
and I finish with a discussion on how early archaeal divisome assembly and curvature
sensing mechanism in bacteria, at first sight unrelated topics, are interconnected
and important groundwork for both fundamental and translational research. "
acknowledged_ssus:
- _id: Bio
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Marko
full_name: Kojic, Marko
id: 73e7ecd4-dc85-11ea-9058-88a16394b160
last_name: Kojic
orcid: 0000-0001-7244-8128
citation:
ama: Kojic M. Towards understanding the assembly mechanisms of the Z-ring in Archaea
and Bacteria. 2025. doi:10.15479/AT-ISTA-20741
apa: Kojic, M. (2025). Towards understanding the assembly mechanisms of the Z-ring
in Archaea and Bacteria. Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20741
chicago: Kojic, Marko. “Towards Understanding the Assembly Mechanisms of the Z-Ring
in Archaea and Bacteria.” Institute of Science and Technology Austria, 2025. https://doi.org/10.15479/AT-ISTA-20741.
ieee: M. Kojic, “Towards understanding the assembly mechanisms of the Z-ring in
Archaea and Bacteria,” Institute of Science and Technology Austria, 2025.
ista: Kojic M. 2025. Towards understanding the assembly mechanisms of the Z-ring
in Archaea and Bacteria. Institute of Science and Technology Austria.
mla: Kojic, Marko. Towards Understanding the Assembly Mechanisms of the Z-Ring
in Archaea and Bacteria. Institute of Science and Technology Austria, 2025,
doi:10.15479/AT-ISTA-20741.
short: M. Kojic, Towards Understanding the Assembly Mechanisms of the Z-Ring in
Archaea and Bacteria, Institute of Science and Technology Austria, 2025.
corr_author: '1'
date_created: 2025-12-09T13:08:11Z
date_published: 2025-12-09T00:00:00Z
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doi: 10.15479/AT-ISTA-20741
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creator: mkojic
date_created: 2025-12-10T13:09:38Z
date_updated: 2025-12-10T13:09:38Z
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file_date_updated: 2025-12-10T13:09:58Z
fulldoi: https://doi.org/10.15479/AT-ISTA-20741
has_accepted_license: '1'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
publication_identifier:
isbn:
- 978-3-99078-073-2
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '15118'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
title: Towards understanding the assembly mechanisms of the Z-ring in Archaea and
Bacteria
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: dissertation
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
year: '2025'
...
---
OA_place: publisher
_id: '20364'
abstract:
- lang: eng
text: "Auxin is a central regulator of plant growth and development, orchestrating
processes from \r\nembryogenesis to senescence through a complex network of biosynthesis,
transport, and \r\nsignaling pathways. \r\nIn Arabidopsis thaliana, canonical
nuclear auxin signaling is mediated by the TIR1/AFB \r\nreceptors, which promote
degradation of AUX/IAA repressors to enable ARF transcription \r\nfactors-driven
transcriptional reprogramming. Parallel to this well-established nuclear \r\nmechanism,
auxin also triggers rapid, non-transcriptional responses. In particular, at the
cell \r\nsurface, most notably through ABP1 and TMKs. Despite decades of research,
the integration \r\nof these pathways and their links to fundamental cellular
processes remains not fully \r\nunderstood. \r\nIn this study, we uncover a new
role for TIR1/AFB signaling in rapidly activating \r\nmacroautophagy during developmental
reprogramming. Auxin induces autophagy via \r\nTIR1/AFB adenylate cyclase activity,
linking auxin perception to cAMP production and \r\ntranscriptional activation
of autophagy machinery. Autophagy-deficient mutants exhibit \r\ndelayed meristem
differentiation, impaired lateral root progression, and reduced shoot \r\norganogenesis,
demonstrating its necessity for timely developmental transitions. \r\nWe also
revisit the ABP1-TMK1 cell-surface auxin perception complex, providing \r\nbiochemical
and mass photometry evidence for auxin-dependent complex formation. We show \r\nthat
ABP1-TMK1 triggers an ultrafast global phosphorylation response targeting ~1000
\r\nproteins, including the auxin transporter PIN2, and Rho-of-plants (ROP) GTPases
regulators. \r\nThis pathway directly regulates PIN2 phosphorylation, for gravitropism
and auxin dependent \r\nROP activation. \r\nThese findings establish an integrated
framework in which nuclear TIR1/AFB signaling and \r\ncell-surface ABP1-TMK signaling
act in parallel to synchronize gene expression, cytoplasmic \r\nremodelling, and
transporter regulation, thereby ensuring robust developmental plasticity in \r\nArabidopsis
thaliana. "
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
acknowledgement: "Plant Facility,\r\nProtein Service Facility"
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
citation:
ama: Giannini C. Nuclear and cell surface auxin signaling in A. thaliana developmental
transitions. 2025. doi:10.15479/AT-ISTA-20364
apa: Giannini, C. (2025). Nuclear and cell surface auxin signaling in A. thaliana
developmental transitions. Institute of Science and Technology Austria. https://doi.org/10.15479/AT-ISTA-20364
chicago: Giannini, Caterina. “Nuclear and Cell Surface Auxin Signaling in A. Thaliana
Developmental Transitions.” Institute of Science and Technology Austria, 2025.
https://doi.org/10.15479/AT-ISTA-20364.
ieee: C. Giannini, “Nuclear and cell surface auxin signaling in A. thaliana developmental
transitions,” Institute of Science and Technology Austria, 2025.
ista: Giannini C. 2025. Nuclear and cell surface auxin signaling in A. thaliana
developmental transitions. Institute of Science and Technology Austria.
mla: Giannini, Caterina. Nuclear and Cell Surface Auxin Signaling in A. Thaliana
Developmental Transitions. Institute of Science and Technology Austria, 2025,
doi:10.15479/AT-ISTA-20364.
short: C. Giannini, Nuclear and Cell Surface Auxin Signaling in A. Thaliana Developmental
Transitions, Institute of Science and Technology Austria, 2025.
corr_author: '1'
date_created: 2025-09-19T12:23:38Z
date_published: 2025-09-19T00:00:00Z
date_updated: 2026-10-16T08:24:09Z
day: '19'
ddc:
- '580'
degree_awarded: PhD
department:
- _id: GradSch
- _id: JiFr
- _id: MaLo
doi: 10.15479/AT-ISTA-20364
doi_confirm: '1'
file:
- access_level: open_access
checksum: 536ba1701453b0b2346be14c046b2911
content_type: application/pdf
creator: cgiannin
date_created: 2025-09-24T14:46:34Z
date_updated: 2026-09-30T22:30:03Z
embargo: 2026-09-30
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file_name: 2025_Giannini_Caterina_Thesis...pdf
file_size: 14278965
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creator: cgiannin
date_created: 2025-09-24T14:46:35Z
date_updated: 2026-09-30T22:30:03Z
embargo_to: open_access
file_id: '20391'
file_name: 2025_Giannini_Caterina_Thesis...docx
file_size: 24499022
relation: source_file
file_date_updated: 2026-09-30T22:30:03Z
fulldoi: https://doi.org/10.15479/AT-ISTA-20364
has_accepted_license: '1'
keyword:
- Auxin Signaling
- Plant Development
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: '151'
publication_identifier:
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '12291'
relation: part_of_dissertation
status: public
- id: '19399'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
title: Nuclear and cell surface auxin signaling in A. thaliana developmental transitions
type: dissertation
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
year: '2025'
...
---
_id: '14834'
abstract:
- lang: eng
text: Bacteria divide by binary fission. The protein machine responsible for this
process is the divisome, a transient assembly of more than 30 proteins in and
on the surface of the cytoplasmic membrane. Together, they constrict the cell
envelope and remodel the peptidoglycan layer to eventually split the cell into
two. For Escherichia coli, most molecular players involved in this process have
probably been identified, but obtaining the quantitative information needed for
a mechanistic understanding can often not be achieved from experiments in vivo
alone. Since the discovery of the Z-ring more than 30 years ago, in vitro reconstitution
experiments have been crucial to shed light on molecular processes normally hidden
in the complex environment of the living cell. In this review, we summarize how
rebuilding the divisome from purified components – or at least parts of it - have
been instrumental to obtain the detailed mechanistic understanding of the bacterial
cell division machinery that we have today.
acknowledgement: We acknowledge members of the Loose laboratory at ISTA for helpful
discussions—in particular M. Kojic for his insightful comments. This work was supported
by the Austrian Science Fund (FWF P34607) to M.L.
article_number: '151380'
article_processing_charge: Yes
article_type: review
author:
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Radler P, Loose M. A dynamic duo: Understanding the roles of FtsZ and FtsA
for Escherichia coli cell division through in vitro approaches. European Journal
of Cell Biology. 2024;103(1). doi:10.1016/j.ejcb.2023.151380'
apa: 'Radler, P., & Loose, M. (2024). A dynamic duo: Understanding the roles
of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches.
European Journal of Cell Biology. Elsevier. https://doi.org/10.1016/j.ejcb.2023.151380'
chicago: 'Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles
of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.”
European Journal of Cell Biology. Elsevier, 2024. https://doi.org/10.1016/j.ejcb.2023.151380.'
ieee: 'P. Radler and M. Loose, “A dynamic duo: Understanding the roles of FtsZ and
FtsA for Escherichia coli cell division through in vitro approaches,” European
Journal of Cell Biology, vol. 103, no. 1. Elsevier, 2024.'
ista: 'Radler P, Loose M. 2024. A dynamic duo: Understanding the roles of FtsZ and
FtsA for Escherichia coli cell division through in vitro approaches. European
Journal of Cell Biology. 103(1), 151380.'
mla: 'Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles
of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.”
European Journal of Cell Biology, vol. 103, no. 1, 151380, Elsevier, 2024,
doi:10.1016/j.ejcb.2023.151380.'
short: P. Radler, M. Loose, European Journal of Cell Biology 103 (2024).
corr_author: '1'
date_created: 2024-01-18T08:16:43Z
date_published: 2024-03-01T00:00:00Z
date_updated: 2025-09-04T11:45:31Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.ejcb.2023.151380
external_id:
isi:
- '001166216800001'
pmid:
- '38218128'
file:
- access_level: open_access
checksum: 5d170abbc87585205c010657e4552360
content_type: application/pdf
creator: dernst
date_created: 2024-07-16T12:07:20Z
date_updated: 2024-07-16T12:07:20Z
file_id: '17265'
file_name: 2024_EJCB_Radler.pdf
file_size: 9995304
relation: main_file
success: 1
file_date_updated: 2024-07-16T12:07:20Z
fulldoi: https://doi.org/10.1016/j.ejcb.2023.151380
has_accepted_license: '1'
intvolume: ' 103'
isi: 1
issue: '1'
keyword:
- Cell Biology
- General Medicine
- Histology
- Pathology and Forensic Medicine
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: In vitro reconstitution of bacterial cell division
publication: European Journal of Cell Biology
publication_identifier:
issn:
- 0171-9335
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli
cell division through in vitro approaches'
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: 103
year: '2024'
...
---
_id: '15118'
abstract:
- lang: eng
text: Cell division in all domains of life requires the orchestration of many proteins,
but in Archaea most of the machinery remains poorly characterized. Here we investigate
the FtsZ-based cell division mechanism in Haloferax volcanii and find proteins
containing photosynthetic reaction centre (PRC) barrel domains that play an essential
role in archaeal cell division. We rename these proteins cell division protein
B 1 (CdpB1) and CdpB2. Depletions and deletions in their respective genes cause
severe cell division defects, generating drastically enlarged cells. Fluorescence
microscopy of tagged FtsZ1, FtsZ2 and SepF in CdpB1 and CdpB2 mutant strains revealed
an unusually disordered divisome that is not organized into a distinct ring-like
structure. Biochemical analysis shows that SepF forms a tripartite complex with
CdpB1/2 and crystal structures suggest that these two proteins might form filaments,
possibly aligning SepF and the FtsZ2 ring during cell division. Overall our results
indicate that PRC-domain proteins play essential roles in FtsZ-based cell division
in Archaea.
acknowledged_ssus:
- _id: LifeSc
acknowledgement: We thank X. Ye (ISTA) for providing the His–SUMO expression plasmid
pSVA13429. pCDB302 was a gift from C. Bahl (Addgene plasmid number 113673; http://n2t.net/addgene:113673;
RRID Addgene_113673). We thank B. Ahsan, G. Sharov, G. Cannone and S. Chen from
the Medical Research Council (MRC) LMB Electron Microscopy Facility for help and
support. We thank Scientific Computing at the MRC LMB for their support. We thank
L. Trübestein and N. Krasnici of the protein service unit of the ISTA Lab Support
Facility for help with the SEC coupled with multi-angle light scattering experiments.
We thank D. Grohmann and R. Reichelt from the Archaea Centre at the University of
Regensburg for providing the P. furiosus cell material. P.N. and S.-V.A. were supported
by a Momentum grant from the Volkswagen (VW) Foundation (grant number 94933). D.K.-C.
and D.B. were supported by the VW Stiftung ‘Life?’ programme (to J.L.; grant number
Az 96727) and by the MRC, as part of UK Research and Innovation (UKRI), MRC file
reference number U105184326 (to J.L.). N.T. and S.G. acknowledge support from the
French Government’s Investissement d’Avenir program, Laboratoire d’Excellence ‘Integrative
Biology of Emerging Infectious Diseases’ (grant number ANR-10-LABX-62-IBEID), and
the computational and storage services (Maestro cluster) provided by the IT department
at Institut Pasteur. M.K. and M.L. were supported by the Austrian Science Fund (FWF)
Stand-Alone P34607. For the purpose of open access, the MRC Laboratory of Molecular
Biology has applied a CC BY public copyright licence to any author accepted manuscript
version arising.
article_processing_charge: No
article_type: original
author:
- first_name: Phillip
full_name: Nußbaum, Phillip
last_name: Nußbaum
- first_name: Danguole
full_name: Kureisaite-Ciziene, Danguole
last_name: Kureisaite-Ciziene
- first_name: Dom
full_name: Bellini, Dom
last_name: Bellini
- first_name: Chris
full_name: Van Der Does, Chris
last_name: Van Der Does
- first_name: Marko
full_name: Kojic, Marko
id: 73e7ecd4-dc85-11ea-9058-88a16394b160
last_name: Kojic
orcid: 0000-0001-7244-8128
- first_name: Najwa
full_name: Taib, Najwa
last_name: Taib
- first_name: Anna
full_name: Yeates, Anna
last_name: Yeates
- first_name: Maxime
full_name: Tourte, Maxime
last_name: Tourte
- first_name: Simonetta
full_name: Gribaldo, Simonetta
last_name: Gribaldo
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Jan
full_name: Löwe, Jan
last_name: Löwe
- first_name: Sonja Verena
full_name: Albers, Sonja Verena
last_name: Albers
citation:
ama: Nußbaum P, Kureisaite-Ciziene D, Bellini D, et al. Proteins containing photosynthetic
reaction centre domains modulate FtsZ-based archaeal cell division. Nature
Microbiology. 2024;9(3):698-711. doi:10.1038/s41564-024-01600-5
apa: Nußbaum, P., Kureisaite-Ciziene, D., Bellini, D., Van Der Does, C., Kojic,
M., Taib, N., … Albers, S. V. (2024). Proteins containing photosynthetic reaction
centre domains modulate FtsZ-based archaeal cell division. Nature Microbiology.
Springer Nature. https://doi.org/10.1038/s41564-024-01600-5
chicago: Nußbaum, Phillip, Danguole Kureisaite-Ciziene, Dom Bellini, Chris Van Der
Does, Marko Kojic, Najwa Taib, Anna Yeates, et al. “Proteins Containing Photosynthetic
Reaction Centre Domains Modulate FtsZ-Based Archaeal Cell Division.” Nature
Microbiology. Springer Nature, 2024. https://doi.org/10.1038/s41564-024-01600-5.
ieee: P. Nußbaum et al., “Proteins containing photosynthetic reaction centre
domains modulate FtsZ-based archaeal cell division,” Nature Microbiology,
vol. 9, no. 3. Springer Nature, pp. 698–711, 2024.
ista: Nußbaum P, Kureisaite-Ciziene D, Bellini D, Van Der Does C, Kojic M, Taib
N, Yeates A, Tourte M, Gribaldo S, Loose M, Löwe J, Albers SV. 2024. Proteins
containing photosynthetic reaction centre domains modulate FtsZ-based archaeal
cell division. Nature Microbiology. 9(3), 698–711.
mla: Nußbaum, Phillip, et al. “Proteins Containing Photosynthetic Reaction Centre
Domains Modulate FtsZ-Based Archaeal Cell Division.” Nature Microbiology,
vol. 9, no. 3, Springer Nature, 2024, pp. 698–711, doi:10.1038/s41564-024-01600-5.
short: P. Nußbaum, D. Kureisaite-Ciziene, D. Bellini, C. Van Der Does, M. Kojic,
N. Taib, A. Yeates, M. Tourte, S. Gribaldo, M. Loose, J. Löwe, S.V. Albers, Nature
Microbiology 9 (2024) 698–711.
date_created: 2024-03-17T23:00:58Z
date_published: 2024-03-04T00:00:00Z
date_updated: 2026-04-07T12:27:57Z
day: '04'
department:
- _id: MaLo
doi: 10.1038/s41564-024-01600-5
external_id:
isi:
- '001183270800021'
pmid:
- '38443575'
fulldoi: https://doi.org/10.1038/s41564-024-01600-5
intvolume: ' 9'
isi: 1
issue: '3'
language:
- iso: eng
month: '03'
oa_version: None
page: 698-711
pmid: 1
project:
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: In vitro reconstitution of bacterial cell division
publication: Nature Microbiology
publication_identifier:
eissn:
- 2058-5276
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
record:
- id: '20741'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Proteins containing photosynthetic reaction centre domains modulate FtsZ-based
archaeal cell division
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 9
year: '2024'
...
---
OA_place: publisher
OA_type: hybrid
_id: '15330'
abstract:
- lang: eng
text: Clathrin-mediated endocytosis (CME) is vital for the regulation of plant growth
and development by controlling plasma membrane protein composition and cargo uptake.
CME relies on the precise recruitment of regulators for vesicle maturation and
release. Homologues of components of mammalian vesicle scission are strong candidates
to be part of the scission machinery in plants, but the precise roles of these
proteins in this process are not fully understood. Here, we characterised the
roles of Plant Dynamin-Related Proteins 2 (DRP2s) and SH3-domain containing protein
2 (SH3P2), the plant homologue to Dynamins’ recruiters, like Endophilin and Amphiphysin,
in the CME by combining high-resolution imaging of endocytic events in vivo and
characterisation of the purified proteins in vitro. Although DRP2s and SH3P2 arrive
similarly late during CME and physically interact, genetic analysis of the sh3p123
triple-mutant and complementation assays with non-SH3P2-interacting DRP2 variants
suggests that SH3P2 does not directly recruit DRP2s to the site of endocytosis.
These observations imply that despite the presence of many well-conserved endocytic
components, plants have acquired a distinct mechanism for CME.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
acknowledgement: "Nataliia Gnyliukh was partially funded by the European Union’s Horizon
2020 research and\r\ninnovation program (2018-2020) under the Marie Sklodowska-Curie
Grant (agreement no.\r\n665385). Taif University Researchers Supporting Project:
TURSP-HC2022/02. and Austrian\r\nScience Fund (FWF): I 6123-B.We thank Prof. Eileen
Lafer and Liping Wang for their suggestions regarding the optimisation of protein
expression and purification. We thank Prof. Sebastian Y. Bednarek for the useful
comments and constructive criticism of the project. We thank Maciek Adamowski for
providing genetic material. This research was supported by the Scientific Service
Units (SSU) of IST-Austria through resources provided by the Electron microscopy
(EMF), Lab Support Facility (LSF) (particularly Dorota Jaworska) and the Bioimaging
Facility (BIF)."
article_number: jcs.261720
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Nataliia
full_name: Gnyliukh, Nataliia
id: 390C1120-F248-11E8-B48F-1D18A9856A87
last_name: Gnyliukh
orcid: 0000-0002-2198-0509
- first_name: Alexander J
full_name: Johnson, Alexander J
id: 46A62C3A-F248-11E8-B48F-1D18A9856A87
last_name: Johnson
orcid: 0000-0002-2739-8843
- first_name: MK
full_name: Nagel, MK
last_name: Nagel
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: David
full_name: Babic, David
id: db566d23-f6e0-11ea-865d-e6f270e968e7
last_name: Babic
- first_name: Annamaria
full_name: Hlavata, Annamaria
id: 36062FEC-F248-11E8-B48F-1D18A9856A87
last_name: Hlavata
- first_name: SS
full_name: Alotaibi, SS
last_name: Alotaibi
- first_name: E
full_name: Isono, E
last_name: Isono
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Gnyliukh N, Johnson AJ, Nagel M, et al. Role of dynamin-related proteins 2
and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana. Journal
of Cell Science. 2024;137(8). doi:10.1242/jcs.261720
apa: Gnyliukh, N., Johnson, A. J., Nagel, M., Monzer, A., Babic, D., Hlavata, A.,
… Friml, J. (2024). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated
endocytosis in Arabidopsis thaliana. Journal of Cell Science. The Company
of Biologists. https://doi.org/10.1242/jcs.261720
chicago: Gnyliukh, Nataliia, Alexander J Johnson, MK Nagel, Aline Monzer, David
Babic, Annamaria Hlavata, SS Alotaibi, E Isono, Martin Loose, and Jiří Friml.
“Role of Dynamin-Related Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis
in Arabidopsis Thaliana.” Journal of Cell Science. The Company of Biologists,
2024. https://doi.org/10.1242/jcs.261720.
ieee: N. Gnyliukh et al., “Role of dynamin-related proteins 2 and SH3P2 in
clathrin-mediated endocytosis in Arabidopsis thaliana,” Journal of Cell Science,
vol. 137, no. 8. The Company of Biologists, 2024.
ista: Gnyliukh N, Johnson AJ, Nagel M, Monzer A, Babic D, Hlavata A, Alotaibi S,
Isono E, Loose M, Friml J. 2024. Role of dynamin-related proteins 2 and SH3P2
in clathrin-mediated endocytosis in Arabidopsis thaliana. Journal of Cell Science.
137(8), jcs. 261720.
mla: Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in
Clathrin-Mediated Endocytosis in Arabidopsis Thaliana.” Journal of Cell Science,
vol. 137, no. 8, jcs. 261720, The Company of Biologists, 2024, doi:10.1242/jcs.261720.
short: N. Gnyliukh, A.J. Johnson, M. Nagel, A. Monzer, D. Babic, A. Hlavata, S.
Alotaibi, E. Isono, M. Loose, J. Friml, Journal of Cell Science 137 (2024).
corr_author: '1'
date_created: 2024-04-19T09:54:59Z
date_published: 2024-04-01T00:00:00Z
date_updated: 2025-09-04T13:49:45Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
- _id: JiFr
- _id: CaBe
doi: 10.1242/jcs.261720
ec_funded: 1
external_id:
isi:
- '001266917100005'
pmid:
- '38506228'
file:
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checksum: 6dc023f0cc7052ad3cf0a42589d2e30f
content_type: application/pdf
creator: dernst
date_created: 2025-01-09T08:41:16Z
date_updated: 2025-01-09T08:41:16Z
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fulldoi: https://doi.org/10.1242/jcs.261720
has_accepted_license: '1'
intvolume: ' 137'
isi: 1
issue: '8'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
- _id: bd76d395-d553-11ed-ba76-f678c14f9033
grant_number: I06123
name: Peptide receptors for auxin canalization in Arabidopsis
publication: Journal of Cell Science
publication_identifier:
eissn:
- 1477-9137
issn:
- 0021-9533
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
related_material:
record:
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relation: earlier_version
status: public
scopus_import: '1'
status: public
title: Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in Arabidopsis thaliana
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: 137
year: '2024'
...
---
OA_place: publisher
OA_type: hybrid
_id: '18938'
abstract:
- lang: eng
text: The synthesis of proteins as encoded in the genome depends critically on translational
fidelity. Nevertheless, errors inevitably occur, and those that result in reading
frame shifts are particularly consequential because the resulting polypeptides
are typically nonfunctional. Despite the generally maladaptive impact of such
errors, the proper decoding of certain mRNAs, including many viral mRNAs, depends
on a process known as programmed ribosomal frameshifting. The fact that these
programmed events, commonly involving a shift to the –1 frame, occur at specific
evolutionarily optimized “slippery” sites has facilitated mechanistic investigation.
By contrast, less is known about the scope and nature of error (i.e., nonprogrammed)
frameshifting. Here, we examine error frameshifting by monitoring spontaneous
frameshift events that suppress the effects of single base pair deletions affecting
two unrelated test proteins. To map the precise sites of frameshifting, we developed
a targeted mass spectrometry–based method called “translational tiling proteomics”
for interrogating the full set of possible –1 slippage events that could produce
the observed frameshift suppression. Surprisingly, such events occur at many sites
along the transcripts, involving up to one half of the available codons. Only
a subset of these resembled canonical “slippery” sites, implicating alternative
mechanisms potentially involving noncognate mispairing events. Additionally, the
aggregate frequency of these events (ranging from 1 to 10% in our test cases)
was higher than we might have anticipated. Our findings point to an unexpected
degree of mechanistic diversity among ribosomal frameshifting events and suggest
that frameshifted products may contribute more significantly to the proteome than
generally assumed.
acknowledgement: We thank S. L. Dove for valuable discussion and comments on the manuscript
and R. Hellmiss for artwork. This work was supported by NIH grants GM136247 to A.H.,
AG011085 to J.W.H., and GM132129 to J.A.P.
article_number: e2317453121
article_processing_charge: No
article_type: original
author:
- first_name: Benjamin L
full_name: Springstein, Benjamin L
id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083
last_name: Springstein
orcid: 0000-0002-3461-5391
- first_name: Joao A.
full_name: Paulo, Joao A.
last_name: Paulo
- first_name: Hankum
full_name: Park, Hankum
last_name: Park
- first_name: Kemardo
full_name: Henry, Kemardo
last_name: Henry
- first_name: Eleanor
full_name: Fleming, Eleanor
last_name: Fleming
- first_name: Zoë
full_name: Feder, Zoë
last_name: Feder
- first_name: J. Wade
full_name: Harper, J. Wade
last_name: Harper
- first_name: Ann
full_name: Hochschild, Ann
last_name: Hochschild
citation:
ama: Springstein BL, Paulo JA, Park H, et al. Systematic analysis of nonprogrammed
frameshift suppression in E.coli via translational tiling proteomics. Proceedings
of the National Academy of Sciences of the United States of America. 2024;121(6).
doi:10.1073/pnas.2317453121
apa: Springstein, B. L., Paulo, J. A., Park, H., Henry, K., Fleming, E., Feder,
Z., … Hochschild, A. (2024). Systematic analysis of nonprogrammed frameshift suppression
in E.coli via translational tiling proteomics. Proceedings of the National
Academy of Sciences of the United States of America. National Academy of Sciences.
https://doi.org/10.1073/pnas.2317453121
chicago: Springstein, Benjamin L, Joao A. Paulo, Hankum Park, Kemardo Henry, Eleanor
Fleming, Zoë Feder, J. Wade Harper, and Ann Hochschild. “Systematic Analysis of
Nonprogrammed Frameshift Suppression in E.Coli via Translational Tiling Proteomics.”
Proceedings of the National Academy of Sciences of the United States of America.
National Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2317453121.
ieee: B. L. Springstein et al., “Systematic analysis of nonprogrammed frameshift
suppression in E.coli via translational tiling proteomics,” Proceedings of
the National Academy of Sciences of the United States of America, vol. 121,
no. 6. National Academy of Sciences, 2024.
ista: Springstein BL, Paulo JA, Park H, Henry K, Fleming E, Feder Z, Harper JW,
Hochschild A. 2024. Systematic analysis of nonprogrammed frameshift suppression
in E.coli via translational tiling proteomics. Proceedings of the National Academy
of Sciences of the United States of America. 121(6), e2317453121.
mla: Springstein, Benjamin L., et al. “Systematic Analysis of Nonprogrammed Frameshift
Suppression in E.Coli via Translational Tiling Proteomics.” Proceedings of
the National Academy of Sciences of the United States of America, vol. 121,
no. 6, e2317453121, National Academy of Sciences, 2024, doi:10.1073/pnas.2317453121.
short: B.L. Springstein, J.A. Paulo, H. Park, K. Henry, E. Fleming, Z. Feder, J.W.
Harper, A. Hochschild, Proceedings of the National Academy of Sciences of the
United States of America 121 (2024).
date_created: 2025-01-29T08:39:27Z
date_published: 2024-02-06T00:00:00Z
date_updated: 2025-05-14T11:02:52Z
day: '06'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1073/pnas.2317453121
external_id:
pmid:
- '38289956'
file:
- access_level: open_access
checksum: 5bd62c7cb4287e3706a1d45d6ef61fd1
content_type: application/pdf
creator: dernst
date_created: 2025-01-29T08:43:16Z
date_updated: 2025-01-29T08:43:16Z
file_id: '18939'
file_name: 2024_PNAS_Springstein.pdf
file_size: 720902
relation: main_file
success: 1
file_date_updated: 2025-01-29T08:43:16Z
fulldoi: https://doi.org/10.1073/pnas.2317453121
has_accepted_license: '1'
intvolume: ' 121'
issue: '6'
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
pmid: 1
publication: Proceedings of the National Academy of Sciences of the United States
of America
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Systematic analysis of nonprogrammed frameshift suppression in E.coli via translational
tiling proteomics
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 121
year: '2024'
...
---
OA_place: publisher
OA_type: gold
_id: '18073'
abstract:
- lang: eng
text: Conserved signaling cascades monitor protein-folding homeostasis to ensure
proper cellular function. One of the evolutionary conserved key players is IRE1,
which maintains endoplasmic reticulum (ER) homeostasis through the unfolded protein
response (UPR). Upon accumulation of misfolded proteins in the ER, IRE1 forms
clusters on the ER membrane to initiate UPR signaling. What regulates IRE1 cluster
formation is not fully understood. Here, we show that the ER lumenal domain (LD)
of human IRE1α forms biomolecular condensates in vitro. IRE1α LD condensates were
stabilized both by binding to unfolded polypeptides as well as by tethering to
model membranes, suggesting their role in assembling IRE1α into signaling-competent
stable clusters. Molecular dynamics simulations indicated that weak multivalent
interactions drive IRE1α LD clustering. Mutagenesis experiments identified disordered
regions in IRE1α LD to control its clustering in vitro and in cells. Importantly,
dysregulated clustering of IRE1α mutants led to defects in IRE1α signaling. Our
results revealed that disordered regions in IRE1α LD control its clustering and
suggest their role as a common strategy in regulating protein assembly on membranes.
acknowledgement: We thank late Thomas Peterbauer at the Max Perutz Labs Biooptics
Light Microscopy Facility for his help and support. We are grateful to Kitti Csalyi
and Thomas Sauer at Max Perutz Labs Biooptics FACS facility for their help. We thank
Grzegorz Scibisz and Sertan Atilla for their support with the expression and purification
of mCherry-IRE1α LD-10His. We are grateful to Aleksandra S Anisimova with her help
in the generation of stable cell lines and the statistical analyses of the data.
We thank Venja Vieweger for her help with the characterization of the WLLI and D123P
IRE1 mutants in cells. We are thankful to Monika Kubickova for the help with the
AUC experiments. We acknowledge CF BIC of CIISB, Instruct-CZ Centre, supported by
MEYS CR (LM2023042)) and European Regional Development Fund-Project, UP CIISB“ (No.
CZ.02.1.01/0.0/0.0/18_046/0015974). We thank the members of the Karagöz lab for
the critical reading and editing of the manuscript. We are thankful to our colleagues
Diego Acosta-Alvear, Vladislav Belyy, Jirka Peschek, Yasin Dagdas, Javier Martinez,
Sascha Martens and Alwin Köhler for their invaluable input on the manuscript. We
are grateful to Life Science Editors, especially Katrina Woolcock for her useful
edits and comments on the manuscript. We acknowledge funding from Austrian Science
Fund (FWF-SFB F79 and FWF-W 1261) to GEK. PK acknowledges the support of the Max
Perutz PhD fellowship. GAV is funded by Stand-Alone grants (P30231-B, P30415-B,
P36572), Special Research Grant (SFB grant F79), and Doctoral School grant (DK grant
W1261) from the Austrian Science Fund (FWF). ES and RC acknowledge support and funding
by the Frankfurt Institute of Advanced Studies, the LOEWE Center for Multiscale
Modelling in Life Sciences of the state of Hesse, the Collaborative Research Center
1507 “Membrane-associated Protein Assemblies, Machineries, and Supercomplexes” (Project
ID 450648163), and the International Max Planck Research School on Cellular Biophysics
(to RC), the Center for Scientific Computing of the Goethe University and the Jülich
Supercomputing Centre for computational resources and support.
article_processing_charge: Yes
article_type: original
author:
- first_name: Paulina
full_name: Kettel, Paulina
last_name: Kettel
- first_name: Laura
full_name: Marosits, Laura
last_name: Marosits
- first_name: Elena
full_name: Spinetti, Elena
last_name: Spinetti
- first_name: Michael
full_name: Rechberger, Michael
last_name: Rechberger
- first_name: Caterina
full_name: Giannini, Caterina
id: e3fdddd5-f6e0-11ea-865d-ca99ee6367f4
last_name: Giannini
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Isabell
full_name: Niedermoser, Isabell
last_name: Niedermoser
- first_name: Irmgard
full_name: Fischer, Irmgard
last_name: Fischer
- first_name: Gijs A.
full_name: Versteeg, Gijs A.
last_name: Versteeg
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Roberto
full_name: Covino, Roberto
last_name: Covino
- first_name: G. Elif
full_name: Karagöz, G. Elif
last_name: Karagöz
citation:
ama: Kettel P, Marosits L, Spinetti E, et al. Disordered regions in the IRE1α ER
lumenal domain mediate its stress-induced clustering. EMBO Journal. 2024;43(20):4668-4698.
doi:10.1038/s44318-024-00207-0
apa: Kettel, P., Marosits, L., Spinetti, E., Rechberger, M., Giannini, C., Radler,
P., … Karagöz, G. E. (2024). Disordered regions in the IRE1α ER lumenal domain
mediate its stress-induced clustering. EMBO Journal. Embo Press. https://doi.org/10.1038/s44318-024-00207-0
chicago: Kettel, Paulina, Laura Marosits, Elena Spinetti, Michael Rechberger, Caterina
Giannini, Philipp Radler, Isabell Niedermoser, et al. “Disordered Regions in the
IRE1α ER Lumenal Domain Mediate Its Stress-Induced Clustering.” EMBO Journal.
Embo Press, 2024. https://doi.org/10.1038/s44318-024-00207-0.
ieee: P. Kettel et al., “Disordered regions in the IRE1α ER lumenal domain
mediate its stress-induced clustering,” EMBO Journal, vol. 43, no. 20.
Embo Press, pp. 4668–4698, 2024.
ista: Kettel P, Marosits L, Spinetti E, Rechberger M, Giannini C, Radler P, Niedermoser
I, Fischer I, Versteeg GA, Loose M, Covino R, Karagöz GE. 2024. Disordered regions
in the IRE1α ER lumenal domain mediate its stress-induced clustering. EMBO Journal.
43(20), 4668–4698.
mla: Kettel, Paulina, et al. “Disordered Regions in the IRE1α ER Lumenal Domain
Mediate Its Stress-Induced Clustering.” EMBO Journal, vol. 43, no. 20,
Embo Press, 2024, pp. 4668–98, doi:10.1038/s44318-024-00207-0.
short: P. Kettel, L. Marosits, E. Spinetti, M. Rechberger, C. Giannini, P. Radler,
I. Niedermoser, I. Fischer, G.A. Versteeg, M. Loose, R. Covino, G.E. Karagöz,
EMBO Journal 43 (2024) 4668–4698.
date_created: 2024-09-15T22:01:42Z
date_published: 2024-10-15T00:00:00Z
date_updated: 2025-09-08T09:22:11Z
day: '15'
ddc:
- '570'
department:
- _id: MaLo
- _id: JiFr
doi: 10.1038/s44318-024-00207-0
external_id:
isi:
- '001306286100002'
pmid:
- '39232130'
file:
- access_level: open_access
checksum: 04f4df1a561083f2846676442fc4eb3c
content_type: application/pdf
creator: dernst
date_created: 2025-01-13T08:43:20Z
date_updated: 2025-01-13T08:43:20Z
file_id: '18827'
file_name: 2024_Embo_Kettel.pdf
file_size: 10080854
relation: main_file
success: 1
file_date_updated: 2025-01-13T08:43:20Z
fulldoi: https://doi.org/10.1038/s44318-024-00207-0
has_accepted_license: '1'
intvolume: ' 43'
isi: 1
issue: '20'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
page: 4668-4698
pmid: 1
publication: EMBO Journal
publication_identifier:
eissn:
- 1460-2075
issn:
- 0261-4189
publication_status: published
publisher: Embo Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced
clustering
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: 43
year: '2024'
...
---
APC_amount: 12348 EUR
OA_place: publisher
OA_type: hybrid
_id: '17460'
abstract:
- lang: eng
text: Filaments in the cell commonly treadmill. Driven by energy consumption, they
grow on one end while shrinking on the other, causing filaments to appear motile
even though individual proteins remain static. This process is characteristic
of cytoskeletal filaments and leads to collective filament self-organization.
Here we show that treadmilling drives filament nematic ordering by dissolving
misaligned filaments. Taking the bacterial FtsZ protein involved in cell division
as an example, we show that this mechanism aligns FtsZ filaments in vitro and
drives the organization of the division ring in living Bacillus subtilis cells.
We find that ordering via local dissolution also allows the system to quickly
respond to chemical and geometrical biases in the cell, enabling us to quantitatively
explain the ring formation dynamics in vivo. Beyond FtsZ and other cytoskeletal
filaments, our study identifies a mechanism for self-organization via constant
birth and death of energy-consuming filaments.
acknowledgement: We thank I. Palaia (ISTA) for useful discussions and K. Lim and R.
W. Wong (WPI-Nano Life Science Institute, Kanazawa University) for providing access
to HS-AFM. We would like to thank B. Prats Mateu (MSD Austria, Vienna) for providing
the HS-AFM data. This work was supported by the Royal Society (grant no. UF160266;
C.V.-C. and A.Š.), the European Union’s Horizon 2020 Research and Innovation Programme
(grant no. 802960; A.Š.), the Austrian Science Fund (FWF) Stand-Alone P34607 (M.L.)
and a Wellcome Trust and Royal Society Sir Henry Dale Fellowship (grant no. 206670/Z/17/Z;
S.H. and K.D.W.).
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Christian Eduardo
full_name: Vanhille-Campos, Christian Eduardo
id: 3adeca52-9313-11ed-b1ac-c170b2505714
last_name: Vanhille-Campos
- first_name: Kevin D.
full_name: Whitley, Kevin D.
last_name: Whitley
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Séamus
full_name: Holden, Séamus
last_name: Holden
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Vanhille-Campos CE, Whitley KD, Radler P, Loose M, Holden S, Šarić A. Self-organization
of mortal filaments and its role in bacterial division ring formation. Nature
Physics. 2024;20:1670-1678. doi:10.1038/s41567-024-02597-8
apa: Vanhille-Campos, C. E., Whitley, K. D., Radler, P., Loose, M., Holden, S.,
& Šarić, A. (2024). Self-organization of mortal filaments and its role in
bacterial division ring formation. Nature Physics. Springer Nature. https://doi.org/10.1038/s41567-024-02597-8
chicago: Vanhille-Campos, Christian Eduardo, Kevin D. Whitley, Philipp Radler, Martin
Loose, Séamus Holden, and Anđela Šarić. “Self-Organization of Mortal Filaments
and Its Role in Bacterial Division Ring Formation.” Nature Physics. Springer
Nature, 2024. https://doi.org/10.1038/s41567-024-02597-8.
ieee: C. E. Vanhille-Campos, K. D. Whitley, P. Radler, M. Loose, S. Holden, and
A. Šarić, “Self-organization of mortal filaments and its role in bacterial division
ring formation,” Nature Physics, vol. 20. Springer Nature, pp. 1670–1678,
2024.
ista: Vanhille-Campos CE, Whitley KD, Radler P, Loose M, Holden S, Šarić A. 2024.
Self-organization of mortal filaments and its role in bacterial division ring
formation. Nature Physics. 20, 1670–1678.
mla: Vanhille-Campos, Christian Eduardo, et al. “Self-Organization of Mortal Filaments
and Its Role in Bacterial Division Ring Formation.” Nature Physics, vol.
20, Springer Nature, 2024, pp. 1670–78, doi:10.1038/s41567-024-02597-8.
short: C.E. Vanhille-Campos, K.D. Whitley, P. Radler, M. Loose, S. Holden, A. Šarić,
Nature Physics 20 (2024) 1670–1678.
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: The simulation data presented in this work are available
from the University College London public data repository at https://doi.org/10.5522/04/24754527
(ref. 74). Live-cell imaging of FtsZ rings data presented in this work are from
ref. 23. High-speed atomic force microscopy data presented in this work are from
ref. 9. Total internal reflection fluorescence microscopy data presented in this
work are from refs. 37,75,76
date_created: 2024-08-25T22:01:08Z
date_published: 2024-10-01T00:00:00Z
date_updated: 2026-09-24T10:58:39Z
day: '01'
ddc:
- '570'
department:
- _id: AnSa
- _id: MaLo
doi: 10.1038/s41567-024-02597-8
ec_funded: 1
external_id:
isi:
- '001289394500005'
pmid:
- '39416851'
file:
- access_level: open_access
checksum: c4842152e2b90d67f48ea8c9ed7c473b
content_type: application/pdf
creator: dernst
date_created: 2025-04-14T06:06:35Z
date_updated: 2025-04-14T06:06:35Z
file_id: '19556'
file_name: 2024_NaturePhysics_VanhilleCampos.pdf
file_size: 8058249
relation: main_file
success: 1
file_date_updated: 2025-04-14T06:06:35Z
fulldoi: https://doi.org/10.1038/s41567-024-02597-8
has_accepted_license: '1'
intvolume: ' 20'
isi: 1
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
page: 1670-1678
pmid: 1
popular_science: '1'
project:
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: In vitro reconstitution of bacterial cell division
- _id: eba2549b-77a9-11ec-83b8-a81e493eae4e
call_identifier: H2020
grant_number: '802960'
name: 'Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines'
publication: Nature Physics
publication_identifier:
eissn:
- 1745-2481
issn:
- 1745-2473
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
record:
- id: '22988'
relation: research_data
status: public
researchdata_availability: yes
scopus_import: '1'
status: public
supplementarymaterial: yes
title: Self-organization of mortal filaments and its role in bacterial division ring
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: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 20
year: '2024'
...
---
OA_place: repository
OA_type: green
_id: '22988'
abstract:
- lang: eng
text: "This repository contains all the necessary files to replicate the simulations
and analyse the data presented in the following publication: \"Self-organization
of mortal filaments and its role in bacterial division ring formation\" - C. Vanhille-Campos
et al. (DOI: https://doi.org/10.1038/s41567-024-02597-8) See README files for
details.\r\n\r\nABSTRACT:\r\n\r\nFilaments in the cell commonly treadmill. Driven
by energy consumption, they grow on one end while shrinking on the other, causing
filaments to appear motile even though individual proteins remain static. This
process is characteristic of cytoskeletal filaments and leads to collective filament
self-organization. Here we show that treadmilling drives filament nematic ordering
by dissolving misaligned filaments. Taking the bacterial FtsZ protein involved
in cell division as an example, we show that this mechanism aligns FtsZ filaments
in vitro and drives the formation of the division ring in living Bacillus subtilis
cells. We find that ordering via local dissolution also allows the system to quickly
respond to chemical and geometrical biases in the cell, enabling us to quantitatively
explain the ring formation dynamics in vivo. Beyond FtsZ and other cytoskeletal
filaments, our study identifies a mechanism for self-organization via constant
birth and death of energy-consuming filaments."
article_processing_charge: No
author:
- first_name: Christian
full_name: Vanhille Campos, Christian
last_name: Vanhille Campos
- first_name: Andela
full_name: Saric, Andela
last_name: Saric
citation:
ama: Vanhille Campos C, Saric A. Self-organization of mortal filaments and its role
in bacterial division ring formation. 2024. doi:10.5522/04/24754527
apa: Vanhille Campos, C., & Saric, A. (2024). Self-organization of mortal filaments
and its role in bacterial division ring formation. Repository. https://doi.org/10.5522/04/24754527
chicago: Vanhille Campos, Christian, and Andela Saric. “Self-Organization of Mortal
Filaments and Its Role in Bacterial Division Ring Formation.” Repository, 2024.
https://doi.org/10.5522/04/24754527.
ieee: C. Vanhille Campos and A. Saric, “Self-organization of mortal filaments and
its role in bacterial division ring formation.” Repository, 2024.
ista: Vanhille Campos C, Saric A. 2024. Self-organization of mortal filaments and
its role in bacterial division ring formation, Repository, 10.5522/04/24754527.
mla: Vanhille Campos, Christian, and Andela Saric. Self-Organization of Mortal
Filaments and Its Role in Bacterial Division Ring Formation. Repository, 2024,
doi:10.5522/04/24754527.
short: C. Vanhille Campos, A. Saric, (2024).
date_created: 2026-09-24T10:56:29Z
date_published: 2024-07-11T00:00:00Z
date_updated: 2026-09-24T10:58:40Z
day: '11'
ddc:
- '570'
department:
- _id: AnSa
- _id: MaLo
doi: 10.5522/04/24754527
fulldoi: https://doi.org/10.5522/04/24754527
main_file_link:
- open_access: '1'
url: https://doi.org/10.5522/04/24754527
month: '07'
oa: 1
oa_version: None
publisher: Repository
related_material:
record:
- id: '17460'
relation: used_in_publication
status: public
status: public
title: Self-organization of mortal filaments and its role in bacterial division ring
formation
type: research_data_reference
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
year: '2024'
...
---
_id: '14795'
abstract:
- lang: eng
text: Metazoan development relies on the formation and remodeling of cell-cell contacts.
Dynamic reorganization of adhesion receptors and the actomyosin cell cortex in
space and time plays a central role in cell-cell contact formation and maturation.
Nevertheless, how this process is mechanistically achieved when new contacts are
formed remains unclear. Here, by building a biomimetic assay composed of progenitor
cells adhering to supported lipid bilayers functionalized with E-cadherin ectodomains,
we show that cortical F-actin flows, driven by the depletion of myosin-2 at the
cell contact center, mediate the dynamic reorganization of adhesion receptors
and cell cortex at the contact. E-cadherin-dependent downregulation of the small
GTPase RhoA at the forming contact leads to both a depletion of myosin-2 and a
decrease of F-actin at the contact center. At the contact rim, in contrast, myosin-2
becomes enriched by the retraction of bleb-like protrusions, resulting in a cortical
tension gradient from the contact rim to its center. This tension gradient, in
turn, triggers centrifugal F-actin flows, leading to further accumulation of F-actin
at the contact rim and the progressive redistribution of E-cadherin from the contact
center to the rim. Eventually, this combination of actomyosin downregulation and
flows at the contact determines the characteristic molecular organization, with
E-cadherin and F-actin accumulating at the contact rim, where they are needed
to mechanically link the contractile cortices of the adhering cells.
acknowledged_ssus:
- _id: Bio
- _id: PreCl
acknowledgement: "We are grateful to Edwin Munro for their feedback and help with
the single particle analysis. We thank members of the Heisenberg and Loose labs
for their help and feedback on the manuscript, notably Xin Tong for making the PCS2-mCherry-AHPH
plasmid. Finally, we thank the Aquatics and Imaging & Optics facilities of ISTA
for their continuous support, especially Yann Cesbron for assistance with the laser
cutter. This work was supported by an ERC\r\nAdvanced Grant (MECSPEC) to C.-P.H."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Feyza N
full_name: Arslan, Feyza N
id: 49DA7910-F248-11E8-B48F-1D18A9856A87
last_name: Arslan
orcid: 0000-0001-5809-9566
- 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: Jack
full_name: Merrin, Jack
id: 4515C308-F248-11E8-B48F-1D18A9856A87
last_name: Merrin
orcid: 0000-0001-5145-4609
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. Adhesion-induced
cortical flows pattern E-cadherin-mediated cell contacts. Current Biology.
2024;34(1):171-182.e8. doi:10.1016/j.cub.2023.11.067
apa: Arslan, F. N., Hannezo, E. B., Merrin, J., Loose, M., & Heisenberg, C.-P.
J. (2024). Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts.
Current Biology. Elsevier. https://doi.org/10.1016/j.cub.2023.11.067
chicago: Arslan, Feyza N, Edouard B Hannezo, Jack Merrin, Martin Loose, and Carl-Philipp
J Heisenberg. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated Cell
Contacts.” Current Biology. Elsevier, 2024. https://doi.org/10.1016/j.cub.2023.11.067.
ieee: F. N. Arslan, E. B. Hannezo, J. Merrin, M. Loose, and C.-P. J. Heisenberg,
“Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts,” Current
Biology, vol. 34, no. 1. Elsevier, p. 171–182.e8, 2024.
ista: Arslan FN, Hannezo EB, Merrin J, Loose M, Heisenberg C-PJ. 2024. Adhesion-induced
cortical flows pattern E-cadherin-mediated cell contacts. Current Biology. 34(1),
171–182.e8.
mla: Arslan, Feyza N., et al. “Adhesion-Induced Cortical Flows Pattern E-Cadherin-Mediated
Cell Contacts.” Current Biology, vol. 34, no. 1, Elsevier, 2024, p. 171–182.e8,
doi:10.1016/j.cub.2023.11.067.
short: F.N. Arslan, E.B. Hannezo, J. Merrin, M. Loose, C.-P.J. Heisenberg, Current
Biology 34 (2024) 171–182.e8.
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: All original microscopy data any additional information
reported in this paper is available from the lead contact upon request. All original
code is available from the lead contact upon request
date_created: 2024-01-14T23:00:56Z
date_published: 2024-01-08T00:00:00Z
date_updated: 2026-10-01T08:33:05Z
day: '08'
ddc:
- '570'
department:
- _id: CaHe
- _id: EdHa
- _id: MaLo
- _id: NanoFab
doi: 10.1016/j.cub.2023.11.067
ec_funded: 1
external_id:
isi:
- '001154500400001'
pmid:
- '38134934'
file:
- access_level: open_access
checksum: 51220b76d72a614208f84bdbfbaf9b72
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T10:53:31Z
date_updated: 2024-01-16T10:53:31Z
file_id: '14813'
file_name: 2024_CurrentBiology_Arslan.pdf
file_size: 5183861
relation: main_file
success: 1
file_date_updated: 2024-01-16T10:53:31Z
fulldoi: https://doi.org/10.1016/j.cub.2023.11.067
has_accepted_license: '1'
intvolume: ' 34'
isi: 1
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
page: 171-182.e8
pmid: 1
project:
- _id: 260F1432-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742573'
name: Interaction and feedback between cell mechanics and fate specification in
vertebrate gastrulation
publication: Current Biology
publication_identifier:
eissn:
- 1879-0445
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
researchdata_availability: upon request
scopus_import: '1'
status: public
supplementarymaterial: yes
title: Adhesion-induced cortical flows pattern E-cadherin-mediated cell contacts
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: 34
year: '2024'
...
---
_id: '15374'
abstract:
- lang: eng
text: Clathrin-mediated endocytosis (CME) is an essential process of cargo uptake
operating in all eukaryotes. In animals and yeast, BAR-SH3 domain proteins, endophilins
and amphiphysins, function at the conclusion of CME to recruit factors for vesicle
scission and uncoating. Arabidopsis thaliana contains the BAR-SH3 domain proteins
SH3P1–SH3P3, but their role is poorly understood. Here, we identify SH3Ps as functional
homologs of endophilin/amphiphysin. SH3P1–SH3P3 bind to discrete foci at the plasma
membrane (PM), and SH3P2 recruits late to a subset of clathrin-coated pits. The
SH3P2 PM recruitment pattern is nearly identical to its interactor, a putative
uncoating factor, AUXILIN-LIKE1. Notably, SH3P1–SH3P3 are required for most of
AUXILIN-LIKE1 recruitment to the PM. This indicates a plant-specific modification
of CME, where BAR-SH3 proteins recruit auxilin-like uncoating factors rather than
the uncoating phosphatases, synaptojanins. SH3P1–SH3P3 act redundantly in overall
CME with the plant-specific endocytic adaptor TPLATE complex but not due to an
SH3 domain in its TASH3 subunit.
acknowledgement: 'The authors wish to acknowledge Dr. Daniel van Damme for mRuby3/pDONRP2rP3
and Prof. Qi-Jun Chen for sharing plasmids used for CRISPR-Cas9 mutagenesis. This
work was supported by the Austrian Science Fund (FWF): I 3630-B25.'
article_number: '114195'
article_processing_charge: Yes
article_type: original
author:
- first_name: Maciek
full_name: Adamowski, Maciek
id: 45F536D2-F248-11E8-B48F-1D18A9856A87
last_name: Adamowski
orcid: 0000-0001-6463-5257
- first_name: Marek
full_name: Randuch, Marek
id: 6ac4636d-15b2-11ec-abd3-fb8df79972ae
last_name: Randuch
- first_name: Ivana
full_name: Matijevic, Ivana
id: 83c17ce3-15b2-11ec-abd3-f486545870bd
last_name: Matijevic
- first_name: Madhumitha
full_name: Narasimhan, Madhumitha
id: 44BF24D0-F248-11E8-B48F-1D18A9856A87
last_name: Narasimhan
orcid: 0000-0002-8600-0671
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
citation:
ama: Adamowski M, Randuch M, Matijevic I, Narasimhan M, Friml J. SH3Ps recruit auxilin-like
vesicle uncoating factors for clathrin-mediated endocytosis. Cell Reports.
2024;43(5). doi:10.1016/j.celrep.2024.114195
apa: Adamowski, M., Randuch, M., Matijevic, I., Narasimhan, M., & Friml, J.
(2024). SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated
endocytosis. Cell Reports. Cell Press. https://doi.org/10.1016/j.celrep.2024.114195
chicago: Adamowski, Maciek, Marek Randuch, Ivana Matijevic, Madhumitha Narasimhan,
and Jiří Friml. “SH3Ps Recruit Auxilin-like Vesicle Uncoating Factors for Clathrin-Mediated
Endocytosis.” Cell Reports. Cell Press, 2024. https://doi.org/10.1016/j.celrep.2024.114195.
ieee: M. Adamowski, M. Randuch, I. Matijevic, M. Narasimhan, and J. Friml, “SH3Ps
recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis,”
Cell Reports, vol. 43, no. 5. Cell Press, 2024.
ista: Adamowski M, Randuch M, Matijevic I, Narasimhan M, Friml J. 2024. SH3Ps recruit
auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis. Cell
Reports. 43(5), 114195.
mla: Adamowski, Maciek, et al. “SH3Ps Recruit Auxilin-like Vesicle Uncoating Factors
for Clathrin-Mediated Endocytosis.” Cell Reports, vol. 43, no. 5, 114195,
Cell Press, 2024, doi:10.1016/j.celrep.2024.114195.
short: M. Adamowski, M. Randuch, I. Matijevic, M. Narasimhan, J. Friml, Cell Reports
43 (2024).
corr_author: '1'
das_tickbox: '1'
dataavailabilitystatement: "All data reported in this paper will be shared by the
lead contact upon request.\r\n\r\nThis paper does not report original code.\r\n\r\nAny
additional information required to reanalyze the data reported in this work paper
is available from the lead contact upon request."
date_created: 2024-05-12T22:01:01Z
date_published: 2024-05-28T00:00:00Z
date_updated: 2026-10-15T08:34:31Z
day: '28'
ddc:
- '580'
department:
- _id: JiFr
- _id: MaLo
doi: 10.1016/j.celrep.2024.114195
external_id:
isi:
- '001240362800001'
pmid:
- '38717900'
file:
- access_level: open_access
checksum: a06bb85be4fc765c51554d27ee2da802
content_type: application/pdf
creator: dernst
date_created: 2024-05-13T12:11:22Z
date_updated: 2024-05-13T12:11:22Z
file_id: '15387'
file_name: 2024_CellReports_Adamowski.pdf
file_size: 5698598
relation: main_file
success: 1
file_date_updated: 2024-05-13T12:11:22Z
fulldoi: https://doi.org/10.1016/j.celrep.2024.114195
has_accepted_license: '1'
intvolume: ' 43'
isi: 1
issue: '5'
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26538374-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03630
name: Molecular mechanisms of endocytic cargo recognition in plants
publication: Cell Reports
publication_identifier:
eissn:
- 2211-1247
publication_status: published
publisher: Cell Press
quality_controlled: '1'
researchdata_availability: upon request
scopus_import: '1'
status: public
supplementarymaterial: yes
title: SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated
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: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 43
year: '2024'
...
---
_id: '12163'
abstract:
- lang: eng
text: Small GTPases play essential roles in the organization of eukaryotic cells.
In recent years, it has become clear that their intracellular functions result
from intricate biochemical networks of the GTPase and their regulators that dynamically
bind to a membrane surface. Due to the inherent complexities of their interactions,
however, revealing the underlying mechanisms of action is often difficult to achieve
from in vivo studies. This review summarizes in vitro reconstitution approaches
developed to obtain a better mechanistic understanding of how small GTPase activities
are regulated in space and time.
acknowledgement: The authors acknowledge support from IST Austria and helpful comments
from the anonymous reviewers that helped to improve this manuscript. We apologize
to the authors of primary literature and outstanding research not cited here due
to space restraints.
article_processing_charge: Yes (via OA deal)
article_type: review
author:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Albert
full_name: Auer, Albert
id: 3018E8C2-F248-11E8-B48F-1D18A9856A87
last_name: Auer
orcid: 0000-0002-3580-2906
- first_name: Gabriel
full_name: Brognara, Gabriel
id: D96FFDA0-A884-11E9-9968-DC26E6697425
last_name: Brognara
- first_name: Hanifatul R
full_name: Budiman, Hanifatul R
id: 55380f95-15b2-11ec-abd3-aff8e230696b
last_name: Budiman
- first_name: Lukasz M
full_name: Kowalski, Lukasz M
id: e3a512e2-4bbe-11eb-a68a-e3857a7844c2
last_name: Kowalski
- first_name: Ivana
full_name: Matijevic, Ivana
id: 83c17ce3-15b2-11ec-abd3-f486545870bd
last_name: Matijevic
citation:
ama: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. In vitro
reconstitution of small GTPase regulation. FEBS Letters. 2023;597(6):762-777.
doi:10.1002/1873-3468.14540
apa: Loose, M., Auer, A., Brognara, G., Budiman, H. R., Kowalski, L. M., & Matijevic,
I. (2023). In vitro reconstitution of small GTPase regulation. FEBS Letters.
Wiley. https://doi.org/10.1002/1873-3468.14540
chicago: Loose, Martin, Albert Auer, Gabriel Brognara, Hanifatul R Budiman, Lukasz
M Kowalski, and Ivana Matijevic. “In Vitro Reconstitution of Small GTPase Regulation.”
FEBS Letters. Wiley, 2023. https://doi.org/10.1002/1873-3468.14540.
ieee: M. Loose, A. Auer, G. Brognara, H. R. Budiman, L. M. Kowalski, and I. Matijevic,
“In vitro reconstitution of small GTPase regulation,” FEBS Letters, vol.
597, no. 6. Wiley, pp. 762–777, 2023.
ista: Loose M, Auer A, Brognara G, Budiman HR, Kowalski LM, Matijevic I. 2023. In
vitro reconstitution of small GTPase regulation. FEBS Letters. 597(6), 762–777.
mla: Loose, Martin, et al. “In Vitro Reconstitution of Small GTPase Regulation.”
FEBS Letters, vol. 597, no. 6, Wiley, 2023, pp. 762–77, doi:10.1002/1873-3468.14540.
short: M. Loose, A. Auer, G. Brognara, H.R. Budiman, L.M. Kowalski, I. Matijevic,
FEBS Letters 597 (2023) 762–777.
corr_author: '1'
date_created: 2023-01-12T12:09:58Z
date_published: 2023-03-01T00:00:00Z
date_updated: 2024-10-09T21:03:42Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1002/1873-3468.14540
external_id:
isi:
- '000891573000001'
pmid:
- '36448231'
file:
- access_level: open_access
checksum: 7492244d3f9c5faa1347ef03f6e5bc84
content_type: application/pdf
creator: dernst
date_created: 2023-08-16T08:31:04Z
date_updated: 2023-08-16T08:31:04Z
file_id: '14063'
file_name: 2023_FEBSLetters_Loose.pdf
file_size: 3148143
relation: main_file
success: 1
file_date_updated: 2023-08-16T08:31:04Z
fulldoi: https://doi.org/10.1002/1873-3468.14540
has_accepted_license: '1'
intvolume: ' 597'
isi: 1
issue: '6'
keyword:
- Cell Biology
- Genetics
- Molecular Biology
- Biochemistry
- Structural Biology
- Biophysics
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
page: 762-777
pmid: 1
publication: FEBS Letters
publication_identifier:
eissn:
- 1873-3468
issn:
- 0014-5793
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: In vitro reconstitution of small GTPase regulation
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 597
year: '2023'
...
---
_id: '14039'
abstract:
- lang: eng
text: Membranes are essential for life. They act as semi-permeable boundaries that
define cells and organelles. In addition, their surfaces actively participate
in biochemical reaction networks, where they confine proteins, align reaction
partners, and directly control enzymatic activities. Membrane-localized reactions
shape cellular membranes, define the identity of organelles, compartmentalize
biochemical processes, and can even be the source of signaling gradients that
originate at the plasma membrane and reach into the cytoplasm and nucleus. The
membrane surface is, therefore, an essential platform upon which myriad cellular
processes are scaffolded. In this review, we summarize our current understanding
of the biophysics and biochemistry of membrane-localized reactions with particular
focus on insights derived from reconstituted and cellular systems. We discuss
how the interplay of cellular factors results in their self-organization, condensation,
assembly, and activity, and the emergent properties derived from them.
acknowledgement: We acknowledge funding from the Austrian Science Fund (FWF F79, P32814-B,
and P35061-B to S.M.; P34607-B to M.L.; and P30584-B and P33066-B to T.A.L.) and
the European Research Council (ERC) under the European Union’s Horizon 2020 research
and innovation program (grant agreement no. 101045340 to M.L.). We are grateful
for comments on the manuscript by Justyna Sawa-Makarska, Verena Baumann, Marko Kojic,
Philipp Radler, Ronja Reinhardt, and Sumire Antonioli.
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Thomas A.
full_name: Leonard, Thomas A.
last_name: Leonard
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Sascha
full_name: Martens, Sascha
last_name: Martens
citation:
ama: Leonard TA, Loose M, Martens S. The membrane surface as a platform that organizes
cellular and biochemical processes. Developmental Cell. 2023;58(15):1315-1332.
doi:10.1016/j.devcel.2023.06.001
apa: Leonard, T. A., Loose, M., & Martens, S. (2023). The membrane surface as
a platform that organizes cellular and biochemical processes. Developmental
Cell. Elsevier. https://doi.org/10.1016/j.devcel.2023.06.001
chicago: Leonard, Thomas A., Martin Loose, and Sascha Martens. “The Membrane Surface
as a Platform That Organizes Cellular and Biochemical Processes.” Developmental
Cell. Elsevier, 2023. https://doi.org/10.1016/j.devcel.2023.06.001.
ieee: T. A. Leonard, M. Loose, and S. Martens, “The membrane surface as a platform
that organizes cellular and biochemical processes,” Developmental Cell,
vol. 58, no. 15. Elsevier, pp. 1315–1332, 2023.
ista: Leonard TA, Loose M, Martens S. 2023. The membrane surface as a platform that
organizes cellular and biochemical processes. Developmental Cell. 58(15), 1315–1332.
mla: Leonard, Thomas A., et al. “The Membrane Surface as a Platform That Organizes
Cellular and Biochemical Processes.” Developmental Cell, vol. 58, no. 15,
Elsevier, 2023, pp. 1315–32, doi:10.1016/j.devcel.2023.06.001.
short: T.A. Leonard, M. Loose, S. Martens, Developmental Cell 58 (2023) 1315–1332.
corr_author: '1'
date_created: 2023-08-13T22:01:12Z
date_published: 2023-08-07T00:00:00Z
date_updated: 2024-10-22T11:40:18Z
day: '07'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.devcel.2023.06.001
external_id:
isi:
- '001059110400001'
pmid:
- '37419118'
file:
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date_created: 2023-08-14T07:57:55Z
date_updated: 2023-08-14T07:57:55Z
file_id: '14049'
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success: 1
file_date_updated: 2023-08-14T07:57:55Z
fulldoi: https://doi.org/10.1016/j.devcel.2023.06.001
has_accepted_license: '1'
intvolume: ' 58'
isi: 1
issue: '15'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
page: 1315-1332
pmid: 1
project:
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: In vitro reconstitution of bacterial cell division
- _id: bd6ae2ca-d553-11ed-ba76-a4aa239da5ee
grant_number: '101045340'
name: Synthetic and structural biology of Rab GTPase networks
publication: Developmental Cell
publication_identifier:
eissn:
- 1878-1551
issn:
- 1534-5807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The membrane surface as a platform that organizes cellular and biochemical
processes
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: 58
year: '2023'
...
---
_id: '14785'
abstract:
- lang: eng
text: Small cryptic plasmids have no clear effect on the host fitness and their
functional repertoire remains obscure. The naturally competent cyanobacterium
Synechocystis sp. PCC 6803 harbours several small cryptic plasmids; whether their
evolution with this species is supported by horizontal transfer remains understudied.
Here, we show that the small cryptic plasmid DNA is transferred in the population
exclusively by natural transformation, where the transfer frequency of plasmid‐encoded
genes is similar to that of chromosome‐encoded genes. Establishing a system to
follow gene transfer, we compared the transfer frequency of genes encoded in cryptic
plasmids pCA2.4 (2378 bp) and pCB2.4 (2345 bp) within and between populations
of two Synechocystis sp. PCC 6803 labtypes (termed
Kiel and Sevilla). Our results reveal that plasmid gene transfer frequency depends
on the recipient labtype. Furthermore, gene transfer via whole plasmid uptake
in the Sevilla labtype ranged among the lowest detected transfer rates in our
experiments. Our study indicates that horizontal DNA transfer via natural transformation
is frequent in the evolution of small cryptic plasmids that reside in naturally
competent organisms. Furthermore, we suggest that the contribution of natural
transformation to cryptic plasmid persistence in Synechocystis is limited.
acknowledgement: "We thank the lab of Francisco Javier Florencio Bel-lido, Sevilla,
Spain for supplying theSynechocystislabtype Sevilla used in this work and the lab
of MartinHagemann, Rostock, Germany for supplying the pIGAplasmidusedinthiswork.WethankNilsHülterforfruitful
discussions. We thank Fenna Stücker forgraphical illustrations and Katrin Schumann,
FennaStücker, and Lidusha Manivannan for technicalsupport.\r\nChilean National
Agency for Research andDevelopment (ANID), Grant/Award Number:21191763; DeutscheForschungsgemeinschaft,
Grant/AwardNumbers: 456882089, RTG2501; EuropeanResearch Council (ERC), Grant/AwardNumber:
101043835"
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Fabian
full_name: Nies, Fabian
last_name: Nies
- first_name: Tanita
full_name: Wein, Tanita
last_name: Wein
- first_name: Dustin M.
full_name: Hanke, Dustin M.
last_name: Hanke
- first_name: Benjamin L
full_name: Springstein, Benjamin L
id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083
last_name: Springstein
orcid: 0000-0002-3461-5391
- first_name: Jaime
full_name: Alcorta, Jaime
last_name: Alcorta
- first_name: Claudia
full_name: Taubenheim, Claudia
last_name: Taubenheim
- first_name: Tal
full_name: Dagan, Tal
last_name: Dagan
citation:
ama: Nies F, Wein T, Hanke DM, et al. Role of natural transformation in the evolution
of small cryptic plasmids in Synechocystis sp. PCC 6803. Environmental Microbiology
Reports. 2023;15(6):656-668. doi:10.1111/1758-2229.13203
apa: Nies, F., Wein, T., Hanke, D. M., Springstein, B. L., Alcorta, J., Taubenheim,
C., & Dagan, T. (2023). Role of natural transformation in the evolution of
small cryptic plasmids in Synechocystis sp. PCC 6803. Environmental Microbiology
Reports. Wiley. https://doi.org/10.1111/1758-2229.13203
chicago: Nies, Fabian, Tanita Wein, Dustin M. Hanke, Benjamin L Springstein, Jaime
Alcorta, Claudia Taubenheim, and Tal Dagan. “Role of Natural Transformation in
the Evolution of Small Cryptic Plasmids in Synechocystis Sp. PCC 6803.” Environmental
Microbiology Reports. Wiley, 2023. https://doi.org/10.1111/1758-2229.13203.
ieee: F. Nies et al., “Role of natural transformation in the evolution of
small cryptic plasmids in Synechocystis sp. PCC 6803,” Environmental Microbiology
Reports, vol. 15, no. 6. Wiley, pp. 656–668, 2023.
ista: Nies F, Wein T, Hanke DM, Springstein BL, Alcorta J, Taubenheim C, Dagan T.
2023. Role of natural transformation in the evolution of small cryptic plasmids
in Synechocystis sp. PCC 6803. Environmental Microbiology Reports. 15(6), 656–668.
mla: Nies, Fabian, et al. “Role of Natural Transformation in the Evolution of Small
Cryptic Plasmids in Synechocystis Sp. PCC 6803.” Environmental Microbiology
Reports, vol. 15, no. 6, Wiley, 2023, pp. 656–68, doi:10.1111/1758-2229.13203.
short: F. Nies, T. Wein, D.M. Hanke, B.L. Springstein, J. Alcorta, C. Taubenheim,
T. Dagan, Environmental Microbiology Reports 15 (2023) 656–668.
date_created: 2024-01-10T10:41:07Z
date_published: 2023-12-01T00:00:00Z
date_updated: 2024-01-16T09:46:12Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1111/1758-2229.13203
external_id:
isi:
- '001080203100001'
pmid:
- '37794696'
file:
- access_level: open_access
checksum: d09ebb68fee61f4e2e09ec286c9cf1d3
content_type: application/pdf
creator: dernst
date_created: 2024-01-16T09:42:10Z
date_updated: 2024-01-16T09:42:10Z
file_id: '14810'
file_name: 2023_EnvirMicroBiolReports_Nies.pdf
file_size: 1518350
relation: main_file
success: 1
file_date_updated: 2024-01-16T09:42:10Z
fulldoi: https://doi.org/10.1111/1758-2229.13203
has_accepted_license: '1'
intvolume: ' 15'
isi: 1
issue: '6'
keyword:
- Agricultural and Biological Sciences (miscellaneous)
- Ecology
- Evolution
- Behavior and Systematics
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
page: 656-668
pmid: 1
publication: Environmental Microbiology Reports
publication_identifier:
eissn:
- 1758-2229
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Role of natural transformation in the evolution of small cryptic plasmids in
Synechocystis sp. PCC 6803
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: 15
year: '2023'
...
---
OA_place: publisher
_id: '14280'
abstract:
- lang: eng
text: "Cell division in Escherichia coli is performed by the divisome, a multi-protein
complex composed of more than 30 proteins. The divisome spans from the cytoplasm
through the inner membrane to the cell wall and the outer membrane. Divisome assembly
is initiated by a cytoskeletal structure, the so-called Z-ring, which localizes
at the center of the E. coli cell and determines the position of the future cell
septum. The Z-ring is composed of the highly conserved bacterial tubulin homologue
FtsZ, which forms treadmilling filaments. These filaments are recruited to the
inner membrane by FtsA, a highly conserved bacterial actin homologue. FtsA interacts
with other proteins in the periplasm and thus connects the cytoplasmic and periplasmic
components of the divisome. \r\nA previous model postulated that FtsA regulates
maturation of the divisome by switching from an oligomeric, inactive state to
a monomeric and active state. This model was based mostly on in vivo studies,
as a biochemical characterization of FtsA has been hampered by difficulties in
purifying the protein. Here, we studied FtsA using an in vitro reconstitution
approach and aimed to answer two questions: (i) How are dynamics from cytoplasmic,
treadmilling FtsZ filaments coupled to proteins acting in the periplasmic space
and (ii) How does FtsA regulate the maturation of the divisome?\r\nWe found that
the cytoplasmic peptides of the transmembrane proteins FtsN and FtsQ interact
directly with FtsA and can follow the spatiotemporal signal of FtsA/Z filaments.
When we investigated the underlying mechanism by imaging single molecules of FtsNcyto,
we found the peptide to interact transiently with FtsA. An in depth analysis of
the single molecule trajectories helped to postulate a model where PG synthases
follow the dynamics of FtsZ by a diffusion and capture mechanism. \r\nFollowing
up on these findings we were interested in how the self-interaction of FtsA changes
when it encounters FtsNcyto and if we can confirm the proposed oligomer-monomer
switch. For this, we compared the behavior of the previously identified, hyperactive
mutant FtsA R286W with wildtype FtsA. The mutant outperforms WT in mirroring and
transmitting the spatiotemporal signal of treadmilling FtsZ filaments. Surprisingly
however, we found that this was not due to a difference in the self-interaction
strength of the two variants, but a difference in their membrane residence time.
Furthermore, in contrast to our expectations, upon binding of FtsNcyto the measured
self-interaction of FtsA actually increased. \r\nWe propose that FtsNcyto induces
a rearrangement of the oligomeric architecture of FtsA. In further consequence
this change leads to more persistent FtsZ filaments which results in a defined
signalling zone, allowing formation of the mature divisome. The observed difference
between FtsA WT and R286W is due to the vastly different membrane turnover of
the proteins. R286W cycles 5-10x faster compared to WT which allows to sample
FtsZ filaments at faster frequencies. These findings can explain the observed
differences in toxicity for overexpression of FtsA WT and R286W and help to understand
how FtsA regulates divisome maturation."
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
citation:
ama: Radler P. Spatiotemporal signaling during assembly of the bacterial divisome.
2023. doi:10.15479/at:ista:14280
apa: Radler, P. (2023). Spatiotemporal signaling during assembly of the bacterial
divisome. Institute of Science and Technology Austria. https://doi.org/10.15479/at:ista:14280
chicago: Radler, Philipp. “Spatiotemporal Signaling during Assembly of the Bacterial
Divisome.” Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/at:ista:14280.
ieee: P. Radler, “Spatiotemporal signaling during assembly of the bacterial divisome,”
Institute of Science and Technology Austria, 2023.
ista: Radler P. 2023. Spatiotemporal signaling during assembly of the bacterial
divisome. Institute of Science and Technology Austria.
mla: Radler, Philipp. Spatiotemporal Signaling during Assembly of the Bacterial
Divisome. Institute of Science and Technology Austria, 2023, doi:10.15479/at:ista:14280.
short: P. Radler, Spatiotemporal Signaling during Assembly of the Bacterial Divisome,
Institute of Science and Technology Austria, 2023.
corr_author: '1'
date_created: 2023-09-06T10:58:25Z
date_published: 2023-09-25T00:00:00Z
date_updated: 2026-04-07T14:06:05Z
day: '25'
ddc:
- '572'
degree_awarded: PhD
department:
- _id: GradSch
- _id: MaLo
doi: 10.15479/at:ista:14280
ec_funded: 1
file:
- access_level: closed
checksum: 87eef11fbc5c7df0826f12a3a629b444
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: pradler
date_created: 2023-10-04T10:11:53Z
date_updated: 2024-10-05T22:30:03Z
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file_name: PhD Thesis_Philipp Radler_20231004.docx
file_size: 114932847
relation: source_file
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checksum: 3253e099b7126469d941fd9419d68b4f
content_type: application/pdf
creator: pradler
date_created: 2023-10-04T10:11:21Z
date_updated: 2024-10-05T22:30:03Z
embargo: 2024-10-04
file_id: '14391'
file_name: PhD Thesis_Philipp Radler_20231004.pdf
file_size: 37838778
relation: main_file
file_date_updated: 2024-10-05T22:30:03Z
fulldoi: https://doi.org/10.15479/at:ista:14280
has_accepted_license: '1'
keyword:
- Cell Division
- Reconstitution
- FtsZ
- FtsA
- Divisome
- E.coli
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: '156'
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: In vitro reconstitution of bacterial cell division
- _id: 2596EAB6-B435-11E9-9278-68D0E5697425
grant_number: ALTF 2015-1163
name: Synthesis of bacterial cell wall
- _id: 259B655A-B435-11E9-9278-68D0E5697425
grant_number: LT000824/2016
name: Reconstitution of bacterial cell wall synthesis
publication_identifier:
isbn:
- 978-3-99078-033-6
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '10934'
relation: research_data
status: public
- id: '11373'
relation: part_of_dissertation
status: public
- id: '7387'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
title: Spatiotemporal signaling during assembly of the bacterial divisome
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: dissertation
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
year: '2023'
...