---
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_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'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '20351'
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'
file:
- access_level: open_access
checksum: a3de801f3c6c1deadd7099d965db799a
content_type: application/pdf
creator: dernst
date_created: 2025-09-15T07:23:12Z
date_updated: 2025-09-15T07:23:12Z
file_id: '20355'
file_name: 2025_ScienceAdvance_Wilmes.pdf
file_size: 3434827
relation: main_file
success: 1
file_date_updated: 2025-09-15T07:23:12Z
fulldoi: https://doi.org/10.1126/sciadv.adx2893
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
issue: '35'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
page: eadx2893
pmid: 1
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
year: '2025'
...
---
_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'
date_created: 2024-01-14T23:00:56Z
date_published: 2024-01-08T00:00:00Z
date_updated: 2025-09-04T11:39:10Z
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'
scopus_import: '1'
status: public
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: '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:
- access_level: open_access
checksum: 6dc023f0cc7052ad3cf0a42589d2e30f
content_type: application/pdf
creator: dernst
date_created: 2025-01-09T08:41:16Z
date_updated: 2025-01-09T08:41:16Z
file_id: '18792'
file_name: 2024_JourCellScience_Gnyliukh.pdf
file_size: 25845948
relation: main_file
success: 1
file_date_updated: 2025-01-09T08:41:16Z
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:
- id: '14591'
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: 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:
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pmid:
- '39232130'
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publisher: Embo Press
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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:
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creator: dernst
date_created: 2025-04-14T06:06:35Z
date_updated: 2025-04-14T06:06:35Z
file_id: '19556'
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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'
...
---
_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:
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checksum: 7492244d3f9c5faa1347ef03f6e5bc84
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creator: dernst
date_created: 2023-08-16T08:31:04Z
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file_id: '14063'
file_name: 2023_FEBSLetters_Loose.pdf
file_size: 3148143
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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
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
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:
- access_level: open_access
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title: The membrane surface as a platform that organizes cellular and biochemical
processes
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text: 'The emergence of large-scale order in self-organized systems relies on local
interactions between individual components. During bacterial cell division, FtsZ
-- a prokaryotic homologue of the eukaryotic protein tubulin -- polymerizes into
treadmilling filaments that further organize into a cytoskeletal ring. In vitro,
FtsZ filaments can form dynamic chiral assemblies. However, how the active and
passive properties of individual filaments relate to these large-scale self-organized
structures remains poorly understood. Here, we connect single filament properties
with the mesoscopic scale by combining minimal active matter simulations and biochemical
reconstitution experiments. We show that density and flexibility of active chiral
filaments define their global order. At intermediate densities, curved, flexible
filaments organize into chiral rings and polar bands. An effectively nematic organization
dominates for high densities and for straight, mutant filaments with increased
rigidity. Our predicted phase diagram captures these features quantitatively,
demonstrating how the flexibility, density and chirality of active filaments affect
their collective behaviour. Our findings shed light on the fundamental properties
of active chiral matter and explain how treadmilling FtsZ filaments organize during
bacterial cell division. '
acknowledged_ssus:
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- _id: LifeSc
acknowledgement: 'This work was supported by the European Research Council through
grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607
to M.L., B. P.M. was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM
collaborative research program. Z.D. has received funding from Doctoral Programme
of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan
Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria),
Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments
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Facility (IOF) and the Lab Support Facility (LSF). '
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ama: Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible
active filaments. 2023. doi:10.15479/AT:ISTA:13116
apa: Dunajova, Z., Prats Mateu, B., Radler, P., Lim, K., Brandis, D., Velicky, P.,
… Loose, M. (2023). Chiral and nematic phases of flexible active filaments. Institute
of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:13116
chicago: Dunajova, Zuzana, Batirtze Prats Mateu, Philipp Radler, Keesiang Lim, Dörte
Brandis, Philipp Velicky, Johann G Danzl, et al. “Chiral and Nematic Phases of
Flexible Active Filaments.” Institute of Science and Technology Austria, 2023.
https://doi.org/10.15479/AT:ISTA:13116.
ieee: Z. Dunajova et al., “Chiral and nematic phases of flexible active filaments.”
Institute of Science and Technology Austria, 2023.
ista: Dunajova Z, Prats Mateu B, Radler P, Lim K, Brandis D, Velicky P, Danzl JG,
Wong RW, Elgeti J, Hannezo EB, Loose M. 2023. Chiral and nematic phases of flexible
active filaments, Institute of Science and Technology Austria, 10.15479/AT:ISTA:13116.
mla: Dunajova, Zuzana, et al. Chiral and Nematic Phases of Flexible Active Filaments.
Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:13116.
short: Z. Dunajova, B. Prats Mateu, P. Radler, K. Lim, D. Brandis, P. Velicky, J.G.
Danzl, R.W. Wong, J. Elgeti, E.B. Hannezo, M. Loose, (2023).
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title: Chiral and nematic phases of flexible active filaments
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abstract:
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text: The emergence of large-scale order in self-organized systems relies on local
interactions between individual components. During bacterial cell division, FtsZ—a
prokaryotic homologue of the eukaryotic protein tubulin—polymerizes into treadmilling
filaments that further organize into a cytoskeletal ring. In vitro, FtsZ filaments
can form dynamic chiral assemblies. However, how the active and passive properties
of individual filaments relate to these large-scale self-organized structures
remains poorly understood. Here we connect single-filament properties with the
mesoscopic scale by combining minimal active matter simulations and biochemical
reconstitution experiments. We show that the density and flexibility of active
chiral filaments define their global order. At intermediate densities, curved,
flexible filaments organize into chiral rings and polar bands. An effectively
nematic organization dominates for high densities and for straight, mutant filaments
with increased rigidity. Our predicted phase diagram quantitatively captures these
features, demonstrating how the flexibility, density and chirality of the active
filaments affect their collective behaviour. Our findings shed light on the fundamental
properties of active chiral matter and explain how treadmilling FtsZ filaments
organize during bacterial cell division.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: 'This work was supported by the European Research Council through
grant ERC 2015-StG-679239 and by the Austrian Science Fund (FWF) StandAlone P34607
to M.L., B. P.M. was also supported by the Kanazawa University WPI- NanoLSI Bio-SPM
collaborative research program. Z.D. has received funding from Doctoral Programme
of the Austrian Academy of Sciences (OeAW): Grant agreement 26360. We thank Jan
Brugues (MPI CBG, Dresden, Germany), Andela Saric (ISTA, Klosterneuburg, Austria),
Daniel Pearce (Uni Geneva, Switzerland) for valuable scientific input and comments
on the manuscript. We are also thankful for the support by the Scientific Service
Units (SSU) of IST Austria through resources provided by the Imaging and Optics
Facility (IOF) and the Lab Support Facility (LSF).'
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citation:
ama: Dunajova Z, Prats Mateu B, Radler P, et al. Chiral and nematic phases of flexible
active filaments. Nature Physics. 2023;19:1916-1926. doi:10.1038/s41567-023-02218-w
apa: Dunajova, Z., Prats Mateu, B., Radler, P., Lim, K., Brandis, D., Velicky, P.,
… Loose, M. (2023). Chiral and nematic phases of flexible active filaments. Nature
Physics. Springer Nature. https://doi.org/10.1038/s41567-023-02218-w
chicago: Dunajova, Zuzana, Batirtze Prats Mateu, Philipp Radler, Keesiang Lim, Dörte
Brandis, Philipp Velicky, Johann G Danzl, et al. “Chiral and Nematic Phases of
Flexible Active Filaments.” Nature Physics. Springer Nature, 2023. https://doi.org/10.1038/s41567-023-02218-w.
ieee: Z. Dunajova et al., “Chiral and nematic phases of flexible active filaments,”
Nature Physics, vol. 19. Springer Nature, pp. 1916–1926, 2023.
ista: Dunajova Z, Prats Mateu B, Radler P, Lim K, Brandis D, Velicky P, Danzl JG,
Wong RW, Elgeti J, Hannezo EB, Loose M. 2023. Chiral and nematic phases of flexible
active filaments. Nature Physics. 19, 1916–1926.
mla: Dunajova, Zuzana, et al. “Chiral and Nematic Phases of Flexible Active Filaments.”
Nature Physics, vol. 19, Springer Nature, 2023, pp. 1916–26, doi:10.1038/s41567-023-02218-w.
short: Z. Dunajova, B. Prats Mateu, P. Radler, K. Lim, D. Brandis, P. Velicky, J.G.
Danzl, R.W. Wong, J. Elgeti, E.B. Hannezo, M. Loose, Nature Physics 19 (2023)
1916–1926.
corr_author: '1'
date_created: 2023-07-27T14:44:45Z
date_published: 2023-12-01T00:00:00Z
date_updated: 2026-09-28T22:30:10Z
day: '01'
ddc:
- '530'
department:
- _id: JoDa
- _id: EdHa
- _id: MaLo
- _id: GradSch
doi: 10.1038/s41567-023-02218-w
ec_funded: 1
external_id:
isi:
- '001178645300041'
pmid:
- '38075437'
file:
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checksum: bc7673ca07d37309013a86166577b2f7
content_type: application/pdf
creator: dernst
date_created: 2024-01-30T14:28:30Z
date_updated: 2024-01-30T14:28:30Z
file_id: '14916'
file_name: 2023_NaturePhysics_Dunajova.pdf
file_size: 22471673
relation: main_file
success: 1
file_date_updated: 2024-01-30T14:28:30Z
fulldoi: https://doi.org/10.1038/s41567-023-02218-w
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intvolume: ' 19'
isi: 1
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
page: 1916-1926
pmid: 1
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: 34d75525-11ca-11ed-8bc3-89b6307fee9d
grant_number: '26360'
name: Motile active matter models of migrating cells and chiral filaments
publication: Nature Physics
publication_identifier:
eissn:
- 1745-2481
issn:
- 1745-2473
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
record:
- id: '13116'
relation: research_data
status: public
- id: '21439'
relation: research_data
status: public
- id: '21423'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Chiral and nematic phases of flexible active filaments
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: 19
year: '2023'
...
---
OA_place: repository
_id: '14591'
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 scissin machinery in plants, but the precise roles of these
proteins in this process is 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 Dsh3p1,2,3
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. One Sentence Summary
In contrast to predictions based on mammalian systems, plant Dynamin-related proteins
2 are recruited to the site of Clathrin-mediated endocytosis independently of
BAR-SH3 proteins.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
article_processing_charge: No
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: Marie-Kristin
full_name: Nagel, Marie-Kristin
last_name: Nagel
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Annamaria
full_name: Hlavata, Annamaria
id: 36062FEC-F248-11E8-B48F-1D18A9856A87
last_name: Hlavata
- first_name: Erika
full_name: Isono, Erika
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-K, et al. Role of dynamin-related proteins
2 and SH3P2 in clathrin-mediated endocytosis in plants. bioRxiv. doi:10.1101/2023.10.09.561523
apa: Gnyliukh, N., Johnson, A. J., Nagel, M.-K., Monzer, A., Hlavata, A., Isono,
E., … Friml, J. (n.d.). Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated
endocytosis in plants. bioRxiv. https://doi.org/10.1101/2023.10.09.561523
chicago: Gnyliukh, Nataliia, Alexander J Johnson, Marie-Kristin Nagel, Aline Monzer,
Annamaria Hlavata, Erika Isono, Martin Loose, and Jiří Friml. “Role of Dynamin-Related
Proteins 2 and SH3P2 in Clathrin-Mediated Endocytosis in Plants.” BioRxiv,
n.d. https://doi.org/10.1101/2023.10.09.561523.
ieee: N. Gnyliukh et al., “Role of dynamin-related proteins 2 and SH3P2 in
clathrin-mediated endocytosis in plants,” bioRxiv. .
ista: Gnyliukh N, Johnson AJ, Nagel M-K, Monzer A, Hlavata A, Isono E, Loose M,
Friml J. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in plants. bioRxiv, 10.1101/2023.10.09.561523.
mla: Gnyliukh, Nataliia, et al. “Role of Dynamin-Related Proteins 2 and SH3P2 in
Clathrin-Mediated Endocytosis in Plants.” BioRxiv, doi:10.1101/2023.10.09.561523.
short: N. Gnyliukh, A.J. Johnson, M.-K. Nagel, A. Monzer, A. Hlavata, E. Isono,
M. Loose, J. Friml, BioRxiv (n.d.).
corr_author: '1'
date_created: 2023-11-22T10:17:49Z
date_published: 2023-10-10T00:00:00Z
date_updated: 2026-09-28T22:30:51Z
day: '10'
department:
- _id: JiFr
- _id: MaLo
- _id: CaBe
doi: 10.1101/2023.10.09.561523
ec_funded: 1
fulldoi: https://doi.org/10.1101/2023.10.09.561523
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2023.10.09.561523
month: '10'
oa: 1
oa_version: Preprint
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
publication: bioRxiv
publication_status: draft
related_material:
record:
- id: '15330'
relation: later_version
status: public
- id: '14510'
relation: dissertation_contains
status: public
status: public
title: Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis
in plants
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '17057'
abstract:
- lang: eng
text: Martin Loose studied chemistry at the University of Heidelberg, Germany. He
then joined Petra Schwille's group at the Max Planck Institute of Molecular Cell
Biology and Genetics in Dresden, where he obtained his PhD degree in 2010 for
work on self-organization and pattern formation in the bacterial Min protein system.
He then moved to Tim Mitchison's lab at Harvard Medical School, Boston, USA for
his postdoc, funded by Human Frontier Science Program (HSFP) and European Molecular
Biology Organization (EMBO) long-term fellowships; there, he discovered that the
bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal
patterns. Martin established his independent research group at the Institute of
Science and Technology (IST) Austria in 2015, supported by an European Research
Council (ERC) starting grant and HFSP Young Investigator Grant. His lab studies
the self-organization of bacterial cell division and small GTPase networks.
article_number: jcs259715
article_processing_charge: No
author:
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Loose M. Cell Scientist to Watch – Martin Loose. Vol 135. The Company
of Biologists; 2022. doi:10.1242/jcs.259715
apa: Loose, M. (2022). Cell scientist to watch – Martin Loose. Journal
of Cell Science (Vol. 135). The Company of Biologists. https://doi.org/10.1242/jcs.259715
chicago: Loose, Martin. Cell Scientist to Watch – Martin Loose. Journal
of Cell Science. Vol. 135. The Company of Biologists, 2022. https://doi.org/10.1242/jcs.259715.
ieee: M. Loose, Cell scientist to watch – Martin Loose, vol. 135, no. 2.
The Company of Biologists, 2022.
ista: Loose M. 2022. Cell scientist to watch – Martin Loose, The Company of Biologists,p.
mla: Loose, Martin. “Cell Scientist to Watch – Martin Loose.” Journal of Cell
Science, vol. 135, no. 2, jcs259715, The Company of Biologists, 2022, doi:10.1242/jcs.259715.
short: M. Loose, Cell Scientist to Watch – Martin Loose, The Company of Biologists,
2022.
date_created: 2024-05-28T13:28:30Z
date_published: 2022-01-19T00:00:00Z
date_updated: 2026-06-18T17:51:26Z
day: '19'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1242/jcs.259715
external_id:
isi:
- '000762665200015'
fulldoi: https://doi.org/10.1242/jcs.259715
intvolume: ' 135'
isi: 1
issue: '2'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1242/jcs.259715
month: '01'
oa: 1
oa_version: Published Version
publication: Journal of Cell Science
publication_identifier:
eissn:
- 1477-9137
issn:
- 0021-9533
publication_status: published
publisher: The Company of Biologists
quality_controlled: '1'
status: public
title: Cell scientist to watch – Martin Loose
type: other_academic_publication
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 135
year: '2022'
...
---
_id: '11373'
abstract:
- lang: eng
text: The actin-homologue FtsA is essential for E. coli cell division, as it links
FtsZ filaments in the Z-ring to transmembrane proteins. FtsA is thought to initiate
cell constriction by switching from an inactive polymeric to an active monomeric
conformation, which recruits downstream proteins and stabilizes the Z-ring. However,
direct biochemical evidence for this mechanism is missing. Here, we use reconstitution
experiments and quantitative fluorescence microscopy to study divisome activation
in vitro. By comparing wild-type FtsA with FtsA R286W, we find that this hyperactive
mutant outperforms FtsA WT in replicating FtsZ treadmilling dynamics, FtsZ filament
stabilization and recruitment of FtsN. We could attribute these differences to
a faster exchange and denser packing of FtsA R286W below FtsZ filaments. Using
FRET microscopy, we also find that FtsN binding promotes FtsA self-interaction.
We propose that in the active divisome FtsA and FtsN exist as a dynamic copolymer
that follows treadmilling filaments of FtsZ.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: We acknowledge members of the Loose laboratory at IST Austria for
helpful discussions—in particular L. Lindorfer for his assistance with cloning and
purifications. We thank J. Löwe and T. Nierhaus (MRC-LMB Cambridge, UK) for sharing
unpublished work and helpful discussions, as well as D. Vavylonis and D. Rutkowski
(Lehigh University, Bethlehem, PA, USA) and S. Martin (University of Lausanne, Switzerland)
for sharing their code for FRAP analysis. We are also thankful for the support by
the Scientific Service Units (SSU) of IST Austria through resources provided by
the Imaging and Optics Facility (IOF) and the Lab Support Facility (LSF). This work
was supported by the European Research Council through grant ERC 2015-StG-679239
and by the Austrian Science Fund (FWF) StandAlone P34607 to M.L. and HFSP LT 000824/2016-L4
to N.B. For the purpose of open access, we have applied a CC BY public copyright
licence to any Author Accepted Manuscript version arising from this submission.
article_number: '2635'
article_processing_charge: No
article_type: original
author:
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: Christoph M
full_name: Sommer, Christoph M
id: 4DF26D8C-F248-11E8-B48F-1D18A9856A87
last_name: Sommer
orcid: 0000-0003-1216-9105
- first_name: Maria D
full_name: Lopez Pelegrin, Maria D
id: 319AA9CE-F248-11E8-B48F-1D18A9856A87
last_name: Lopez Pelegrin
- first_name: David
full_name: Michalik, David
id: B9577E20-AA38-11E9-AC9A-0930E6697425
last_name: Michalik
- 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, Baranova NS, Dos Santos Caldas PR, et al. In vitro reconstitution
of Escherichia coli divisome activation. Nature Communications. 2022;13.
doi:10.1038/s41467-022-30301-y
apa: Radler, P., Baranova, N. S., Dos Santos Caldas, P. R., Sommer, C. M., Lopez
Pelegrin, M. D., Michalik, D., & Loose, M. (2022). In vitro reconstitution
of Escherichia coli divisome activation. Nature Communications. Springer
Nature. https://doi.org/10.1038/s41467-022-30301-y
chicago: Radler, Philipp, Natalia S. Baranova, Paulo R Dos Santos Caldas, Christoph
M Sommer, Maria D Lopez Pelegrin, David Michalik, and Martin Loose. “In Vitro
Reconstitution of Escherichia Coli Divisome Activation.” Nature Communications.
Springer Nature, 2022. https://doi.org/10.1038/s41467-022-30301-y.
ieee: P. Radler et al., “In vitro reconstitution of Escherichia coli divisome
activation,” Nature Communications, vol. 13. Springer Nature, 2022.
ista: Radler P, Baranova NS, Dos Santos Caldas PR, Sommer CM, Lopez Pelegrin MD,
Michalik D, Loose M. 2022. In vitro reconstitution of Escherichia coli divisome
activation. Nature Communications. 13, 2635.
mla: Radler, Philipp, et al. “In Vitro Reconstitution of Escherichia Coli Divisome
Activation.” Nature Communications, vol. 13, 2635, Springer Nature, 2022,
doi:10.1038/s41467-022-30301-y.
short: P. Radler, N.S. Baranova, P.R. Dos Santos Caldas, C.M. Sommer, M.D. Lopez
Pelegrin, D. Michalik, M. Loose, Nature Communications 13 (2022).
corr_author: '1'
date_created: 2022-05-13T09:06:28Z
date_published: 2022-05-12T00:00:00Z
date_updated: 2026-09-28T22:30:07Z
day: '12'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1038/s41467-022-30301-y
ec_funded: 1
external_id:
isi:
- '000795171100037'
file:
- access_level: open_access
checksum: 5af863ee1b95a0710f6ee864d68dc7a6
content_type: application/pdf
creator: dernst
date_created: 2022-05-13T09:10:51Z
date_updated: 2022-05-13T09:10:51Z
file_id: '11374'
file_name: 2022_NatureCommunications_Radler.pdf
file_size: 6945191
relation: main_file
success: 1
file_date_updated: 2022-05-13T09:10:51Z
fulldoi: https://doi.org/10.1038/s41467-022-30301-y
has_accepted_license: '1'
intvolume: ' 13'
isi: 1
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
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
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41467-022-34485-1
record:
- id: '10934'
relation: research_data
status: public
- id: '14280'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: In vitro reconstitution of Escherichia coli divisome activation
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 13
year: '2022'
...
---
_id: '8988'
abstract:
- lang: eng
text: The differentiation of cells depends on a precise control of their internal
organization, which is the result of a complex dynamic interplay between the cytoskeleton,
molecular motors, signaling molecules, and membranes. For example, in the developing
neuron, the protein ADAP1 (ADP-ribosylation factor GTPase-activating protein [ArfGAP]
with dual pleckstrin homology [PH] domains 1) has been suggested to control dendrite
branching by regulating the small GTPase ARF6. Together with the motor protein
KIF13B, ADAP1 is also thought to mediate delivery of the second messenger phosphatidylinositol
(3,4,5)-trisphosphate (PIP3) to the axon tip, thus contributing to PIP3 polarity.
However, what defines the function of ADAP1 and how its different roles are coordinated
are still not clear. Here, we studied ADAP1’s functions using in vitro reconstitutions.
We found that KIF13B transports ADAP1 along microtubules, but that PIP3 as well
as PI(3,4)P2 act as stop signals for this transport instead of being transported.
We also demonstrate that these phosphoinositides activate ADAP1’s enzymatic activity
to catalyze GTP hydrolysis by ARF6. Together, our results support a model for
the cellular function of ADAP1, where KIF13B transports ADAP1 until it encounters
high PIP3/PI(3,4)P2 concentrations in the plasma membrane. Here, ADAP1 disassociates
from the motor to inactivate ARF6, promoting dendrite branching.
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
- _id: EM-Fac
acknowledgement: "We thank Urban Bezeljak, Natalia Baranova, Mar Lopez-Pelegrin, Catarina
Alcarva, and Victoria Faas for sharing reagents and helpful discussions. We thank
Veronika Szentirmai for help with protein purifications. We thank Carrie Bernecky,
Sascha Martens, and the M.L. lab for comments on the manuscript. We thank the bioimaging
facility, the life science facility, and Armel Nicolas from the mass spec facility
at the Institute of Science and Technology (IST) Austria for technical support.
C.D. acknowledges funding from the IST fellowship program; this work was supported
by Human Frontier Science Program Young Investigator Grant\r\nRGY0083/2016. "
article_number: e2010054118
article_processing_charge: No
article_type: original
author:
- first_name: Christian F
full_name: Düllberg, Christian F
id: 459064DC-F248-11E8-B48F-1D18A9856A87
last_name: Düllberg
orcid: 0000-0001-6335-9748
- first_name: Albert
full_name: Auer, Albert
id: 3018E8C2-F248-11E8-B48F-1D18A9856A87
last_name: Auer
orcid: 0000-0002-3580-2906
- first_name: Nikola
full_name: Canigova, Nikola
id: 3795523E-F248-11E8-B48F-1D18A9856A87
last_name: Canigova
orcid: 0000-0002-8518-5926
- first_name: Katrin
full_name: Loibl, Katrin
id: 3760F32C-F248-11E8-B48F-1D18A9856A87
last_name: Loibl
orcid: 0000-0002-2429-7668
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Düllberg CF, Auer A, Canigova N, Loibl K, Loose M. In vitro reconstitution
reveals phosphoinositides as cargo-release factors and activators of the ARF6
GAP ADAP1. Proceedings of the National Academy of Sciences of the United States
of America. 2021;118(1). doi:10.1073/pnas.2010054118
apa: Düllberg, C. F., Auer, A., Canigova, N., Loibl, K., & Loose, M. (2021).
In vitro reconstitution reveals phosphoinositides as cargo-release factors and
activators of the ARF6 GAP ADAP1. Proceedings of the National Academy of Sciences
of the United States of America. National Academy of Sciences. https://doi.org/10.1073/pnas.2010054118
chicago: Düllberg, Christian F, Albert Auer, Nikola Canigova, Katrin Loibl, and
Martin Loose. “In Vitro Reconstitution Reveals Phosphoinositides as Cargo-Release
Factors and Activators of the ARF6 GAP ADAP1.” Proceedings of the National
Academy of Sciences of the United States of America. National Academy of Sciences,
2021. https://doi.org/10.1073/pnas.2010054118.
ieee: C. F. Düllberg, A. Auer, N. Canigova, K. Loibl, and M. Loose, “In vitro reconstitution
reveals phosphoinositides as cargo-release factors and activators of the ARF6
GAP ADAP1,” Proceedings of the National Academy of Sciences of the United States
of America, vol. 118, no. 1. National Academy of Sciences, 2021.
ista: Düllberg CF, Auer A, Canigova N, Loibl K, Loose M. 2021. In vitro reconstitution
reveals phosphoinositides as cargo-release factors and activators of the ARF6
GAP ADAP1. Proceedings of the National Academy of Sciences of the United States
of America. 118(1), e2010054118.
mla: Düllberg, Christian F., et al. “In Vitro Reconstitution Reveals Phosphoinositides
as Cargo-Release Factors and Activators of the ARF6 GAP ADAP1.” Proceedings
of the National Academy of Sciences of the United States of America, vol.
118, no. 1, e2010054118, National Academy of Sciences, 2021, doi:10.1073/pnas.2010054118.
short: C.F. Düllberg, A. Auer, N. Canigova, K. Loibl, M. Loose, Proceedings of the
National Academy of Sciences of the United States of America 118 (2021).
corr_author: '1'
date_created: 2021-01-03T23:01:23Z
date_published: 2021-01-05T00:00:00Z
date_updated: 2026-06-18T19:37:53Z
day: '05'
ddc:
- '570'
department:
- _id: MaLo
- _id: MiSi
doi: 10.1073/pnas.2010054118
external_id:
isi:
- '000607270100018'
pmid:
- '33443153'
fulldoi: https://doi.org/10.1073/pnas.2010054118
intvolume: ' 118'
isi: 1
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.2010054118
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 2599F062-B435-11E9-9278-68D0E5697425
grant_number: RGY0083/2016
name: Reconstitution of cell polarity and axis determination in a cell-free system
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: In vitro reconstitution reveals phosphoinositides as cargo-release factors
and activators of the ARF6 GAP ADAP1
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 118
year: '2021'
...
---
_id: '9243'
abstract:
- lang: eng
text: Peptidoglycan is an essential component of the bacterial cell envelope that
surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important
antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis.
Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan
synthases that polymerize glycan chains and connect adjacent stem peptides by
transpeptidation. How these enzymes work in their physiological membrane environment
is poorly understood. Here, we developed a novel Förster resonance energy transfer-based
assay to follow in real time both reactions of class A PBPs reconstituted in liposomes
or supported lipid bilayers and applied this assay with PBP1B homologues from
Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii in the presence
or absence of their cognate lipoprotein activator. Our assay will allow unravelling
the mechanisms of peptidoglycan synthesis in a lipid-bilayer environment and can
be further developed to be used for high-throughput screening for new antimicrobials.
acknowledgement: 'We thank Alexander Egan (Newcastle University) for purified proteins
LpoB(sol) and LpoPPa(sol), Federico Corona (Newcastle University) for purified MepM,
and Oliver Birkholz and Jacob Piehler (Department of Biology and Center of Cellular
Nanoanalytics, University of Osnabru¨ ck) for their help with PBP1B reconstitution
into polymer-SLBs and initial guidance on single particle tracking. We also acknowledge
Christian P Richter and Changjiang You (Department of Biology and Center of Cellular
Nanoanalytics, University of Osnabru¨ ck) for providing SLIMfast software and tris-DODA-NTA
reagent, respectively. This work was funded by the BBSRC grant BB/R017409/1 (to
WV), the European Research Council through grant ERC-2015-StG-679239 (to ML), and
long-term fellowships HFSP LT 000824/2016-L4 and EMBO ALTF 1163–2015 (to NB). '
article_number: 1-32
article_processing_charge: No
article_type: original
author:
- first_name: Víctor M.
full_name: Hernández-Rocamora, Víctor M.
last_name: Hernández-Rocamora
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Katharina
full_name: Peters, Katharina
last_name: Peters
- first_name: Eefjan
full_name: Breukink, Eefjan
last_name: Breukink
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Waldemar
full_name: Vollmer, Waldemar
last_name: Vollmer
citation:
ama: Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer
W. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin
binding proteins. eLife. 2021;10. doi:10.7554/eLife.61525
apa: Hernández-Rocamora, V. M., Baranova, N. S., Peters, K., Breukink, E., Loose,
M., & Vollmer, W. (2021). Real time monitoring of peptidoglycan synthesis
by membrane-reconstituted penicillin binding proteins. ELife. eLife Sciences
Publications. https://doi.org/10.7554/eLife.61525
chicago: Hernández-Rocamora, Víctor M., Natalia S. Baranova, Katharina Peters, Eefjan
Breukink, Martin Loose, and Waldemar Vollmer. “Real Time Monitoring of Peptidoglycan
Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” ELife.
eLife Sciences Publications, 2021. https://doi.org/10.7554/eLife.61525.
ieee: V. M. Hernández-Rocamora, N. S. Baranova, K. Peters, E. Breukink, M. Loose,
and W. Vollmer, “Real time monitoring of peptidoglycan synthesis by membrane-reconstituted
penicillin binding proteins,” eLife, vol. 10. eLife Sciences Publications,
2021.
ista: Hernández-Rocamora VM, Baranova NS, Peters K, Breukink E, Loose M, Vollmer
W. 2021. Real time monitoring of peptidoglycan synthesis by membrane-reconstituted
penicillin binding proteins. eLife. 10, 1–32.
mla: Hernández-Rocamora, Víctor M., et al. “Real Time Monitoring of Peptidoglycan
Synthesis by Membrane-Reconstituted Penicillin Binding Proteins.” ELife,
vol. 10, 1–32, eLife Sciences Publications, 2021, doi:10.7554/eLife.61525.
short: V.M. Hernández-Rocamora, N.S. Baranova, K. Peters, E. Breukink, M. Loose,
W. Vollmer, ELife 10 (2021).
date_created: 2021-03-14T23:01:33Z
date_published: 2021-02-24T00:00:00Z
date_updated: 2024-10-22T10:04:21Z
day: '24'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.7554/eLife.61525
ec_funded: 1
external_id:
isi:
- '000627596400001'
file:
- access_level: open_access
checksum: 79897a09bfecd9914d39c4aea2841855
content_type: application/pdf
creator: dernst
date_created: 2021-03-22T07:36:08Z
date_updated: 2021-03-22T07:36:08Z
file_id: '9268'
file_name: 2021_eLife_HernandezRocamora.pdf
file_size: 2314698
relation: main_file
success: 1
file_date_updated: 2021-03-22T07:36:08Z
fulldoi: https://doi.org/10.7554/eLife.61525
has_accepted_license: '1'
intvolume: ' 10'
isi: 1
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _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: eLife
publication_identifier:
eissn:
- 2050-084X
publication_status: published
publisher: eLife Sciences Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Real time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin
binding proteins
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 10
year: '2021'
...
---
_id: '9414'
abstract:
- lang: eng
text: Microtubule plus-end depolymerization rate is a potentially important target
of physiological regulation, but it has been challenging to measure, so its role
in spatial organization is poorly understood. Here we apply a method for tracking
plus ends based on time difference imaging to measure depolymerization rates in
large interphase asters growing in Xenopus egg extract. We observed strong spatial
regulation of depolymerization rates, which were higher in the aster interior
compared with the periphery, and much less regulation of polymerization or catastrophe
rates. We interpret these data in terms of a limiting component model, where aster
growth results in lower levels of soluble tubulin and microtubule-associated proteins
(MAPs) in the interior cytosol compared with that at the periphery. The steady-state
polymer fraction of tubulin was ∼30%, so tubulin is not strongly depleted in the
aster interior. We propose that the limiting component for microtubule assembly
is a MAP that inhibits depolymerization, and that egg asters are tuned to low
microtubule density.
acknowledgement: The authors thank the members of Mitchison, Brugués, and Jay Gatlin
groups (University of Wyoming) for discussions. We thank Heino Andreas (MPI-CBG)
for frog maintenance. We thank Nikon for microscopy support at Marine Biological
Laboratory (MBL). K.I. was supported by fellowships from the Honjo International
Scholarship Foundation and Center of Systems Biology Dresden. F.D. was supported
by the DIGGS-BB fellowship provided by the German Research Foundation (DFG). P.C.
is supported by a Boehringer Ingelheim Fonds PhD fellowship. J.F.P. was supported
by a fellowship from the Fannie and John Hertz Foundation. M.L.’s research is supported
by European Research Council (ERC) Grant no. ERC-2015-StG-679239. J.B.’s research
is supported by the Human Frontiers Science Program (CDA00074/2014). T.J.M.’s research
is supported by National Institutes of Health Grant no. R35GM131753.
article_processing_charge: No
article_type: original
author:
- first_name: Keisuke
full_name: Ishihara, Keisuke
last_name: Ishihara
- first_name: Franziska
full_name: Decker, Franziska
last_name: Decker
- first_name: Paulo R
full_name: Dos Santos Caldas, Paulo R
id: 38FCDB4C-F248-11E8-B48F-1D18A9856A87
last_name: Dos Santos Caldas
orcid: 0000-0001-6730-4461
- first_name: James F.
full_name: Pelletier, James F.
last_name: Pelletier
- 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: Brugués, Jan
last_name: Brugués
- first_name: Timothy J.
full_name: Mitchison, Timothy J.
last_name: Mitchison
citation:
ama: Ishihara K, Decker F, Dos Santos Caldas PR, et al. Spatial variation of microtubule
depolymerization in large asters. Molecular Biology of the Cell. 2021;32(9):869-879.
doi:10.1091/MBC.E20-11-0723
apa: Ishihara, K., Decker, F., Dos Santos Caldas, P. R., Pelletier, J. F., Loose,
M., Brugués, J., & Mitchison, T. J. (2021). Spatial variation of microtubule
depolymerization in large asters. Molecular Biology of the Cell. American
Society for Cell Biology. https://doi.org/10.1091/MBC.E20-11-0723
chicago: Ishihara, Keisuke, Franziska Decker, Paulo R Dos Santos Caldas, James F.
Pelletier, Martin Loose, Jan Brugués, and Timothy J. Mitchison. “Spatial Variation
of Microtubule Depolymerization in Large Asters.” Molecular Biology of the
Cell. American Society for Cell Biology, 2021. https://doi.org/10.1091/MBC.E20-11-0723.
ieee: K. Ishihara et al., “Spatial variation of microtubule depolymerization
in large asters,” Molecular Biology of the Cell, vol. 32, no. 9. American
Society for Cell Biology, pp. 869–879, 2021.
ista: Ishihara K, Decker F, Dos Santos Caldas PR, Pelletier JF, Loose M, Brugués
J, Mitchison TJ. 2021. Spatial variation of microtubule depolymerization in large
asters. Molecular Biology of the Cell. 32(9), 869–879.
mla: Ishihara, Keisuke, et al. “Spatial Variation of Microtubule Depolymerization
in Large Asters.” Molecular Biology of the Cell, vol. 32, no. 9, American
Society for Cell Biology, 2021, pp. 869–79, doi:10.1091/MBC.E20-11-0723.
short: K. Ishihara, F. Decker, P.R. Dos Santos Caldas, J.F. Pelletier, M. Loose,
J. Brugués, T.J. Mitchison, Molecular Biology of the Cell 32 (2021) 869–879.
date_created: 2021-05-23T22:01:45Z
date_published: 2021-04-19T00:00:00Z
date_updated: 2026-06-18T19:52:16Z
day: '19'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1091/MBC.E20-11-0723
ec_funded: 1
external_id:
isi:
- '000641574700005'
pmid:
- '33439671'
fulldoi: https://doi.org/10.1091/MBC.E20-11-0723
intvolume: ' 32'
isi: 1
issue: '9'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-sa/3.0/
main_file_link:
- open_access: '1'
url: https://www.molbiolcell.org/doi/10.1091/mbc.E20-11-0723
month: '04'
oa: 1
oa_version: Published Version
page: 869-879
pmid: 1
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
- _id: 260D98C8-B435-11E9-9278-68D0E5697425
name: Reconstitution of Bacterial Cell Division Using Purified Components
publication: Molecular Biology of the Cell
publication_identifier:
eissn:
- 1939-4586
issn:
- 1059-1524
publication_status: published
publisher: American Society for Cell Biology
quality_controlled: '1'
scopus_import: '1'
status: public
title: Spatial variation of microtubule depolymerization in large asters
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/3.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported (CC BY-NC-SA
3.0)
short: CC BY-NC-SA (3.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2021'
...
---
_id: '9907'
abstract:
- lang: eng
text: 'DivIVA is a protein initially identified as a spatial regulator of cell division
in the model organism Bacillus subtilis, but its homologues are present in many
other Gram-positive bacteria, including Clostridia species. Besides its role as
topological regulator of the Min system during bacterial cell division, DivIVA
is involved in chromosome segregation during sporulation, genetic competence,
and cell wall synthesis. DivIVA localizes to regions of high membrane curvature,
such as the cell poles and cell division site, where it recruits distinct binding
partners. Previously, it was suggested that negative curvature sensing is the
main mechanism by which DivIVA binds to these specific regions. Here, we show
that Clostridioides difficile DivIVA binds preferably to membranes containing
negatively charged phospholipids, especially cardiolipin. Strikingly, we observed
that upon binding, DivIVA modifies the lipid distribution and induces changes
to lipid bilayers containing cardiolipin. Our observations indicate that DivIVA
might play a more complex and so far unknown active role during the formation
of the cell division septal membrane. '
acknowledged_ssus:
- _id: Bio
- _id: LifeSc
acknowledgement: "We thank Daniela Krajˇcíkova, Katarína Muchová, Zuzana Chromíkova
and other members of Barák’s laboratory for useful discussions, suggestions and
help. Special thanks also to Emília Chovancová for technical support. We are grateful
to Juraj Labaj for drawing the model and for help with graphics. Many thanks to
all members of Loose’s laboratory: Maria del Mar\r\nLópez, Paulo Caldas, Philipp
Radler, and other members of the Loose’s laboratory for sharing their knowledge
of SLB preparation and TIRF experiment chambers, for sharing coverslips and for
help with the TIRF microscope and data analysis. We also thank the members of the
Dept. of Biochemistry of Biomembranes at the Institute of Animal Biochemistry and
Genetics, CBs SAS for their help with preparing the lipid mixtures. We thank J.
Bauer for critically reading the manuscript."
article_number: '8350'
article_processing_charge: Yes
article_type: original
author:
- first_name: Naďa
full_name: Labajová, Naďa
last_name: Labajová
- first_name: Natalia S.
full_name: Baranova, Natalia S.
id: 38661662-F248-11E8-B48F-1D18A9856A87
last_name: Baranova
orcid: 0000-0002-3086-9124
- first_name: Miroslav
full_name: Jurásek, Miroslav
last_name: Jurásek
- first_name: Robert
full_name: Vácha, Robert
last_name: Vácha
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
- first_name: Imrich
full_name: Barák, Imrich
last_name: Barák
citation:
ama: Labajová N, Baranova NS, Jurásek M, Vácha R, Loose M, Barák I. Cardiolipin-containing
lipid membranes attract the bacterial cell division protein diviva. International
Journal of Molecular Sciences. 2021;22(15). doi:10.3390/ijms22158350
apa: Labajová, N., Baranova, N. S., Jurásek, M., Vácha, R., Loose, M., & Barák,
I. (2021). Cardiolipin-containing lipid membranes attract the bacterial cell division
protein diviva. International Journal of Molecular Sciences. MDPI. https://doi.org/10.3390/ijms22158350
chicago: Labajová, Naďa, Natalia S. Baranova, Miroslav Jurásek, Robert Vácha, Martin
Loose, and Imrich Barák. “Cardiolipin-Containing Lipid Membranes Attract the Bacterial
Cell Division Protein Diviva.” International Journal of Molecular Sciences.
MDPI, 2021. https://doi.org/10.3390/ijms22158350.
ieee: N. Labajová, N. S. Baranova, M. Jurásek, R. Vácha, M. Loose, and I. Barák,
“Cardiolipin-containing lipid membranes attract the bacterial cell division protein
diviva,” International Journal of Molecular Sciences, vol. 22, no. 15.
MDPI, 2021.
ista: Labajová N, Baranova NS, Jurásek M, Vácha R, Loose M, Barák I. 2021. Cardiolipin-containing
lipid membranes attract the bacterial cell division protein diviva. International
Journal of Molecular Sciences. 22(15), 8350.
mla: Labajová, Naďa, et al. “Cardiolipin-Containing Lipid Membranes Attract the
Bacterial Cell Division Protein Diviva.” International Journal of Molecular
Sciences, vol. 22, no. 15, 8350, MDPI, 2021, doi:10.3390/ijms22158350.
short: N. Labajová, N.S. Baranova, M. Jurásek, R. Vácha, M. Loose, I. Barák, International
Journal of Molecular Sciences 22 (2021).
date_created: 2021-08-15T22:01:27Z
date_published: 2021-08-01T00:00:00Z
date_updated: 2025-07-10T12:02:05Z
day: '01'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.3390/ijms22158350
ec_funded: 1
external_id:
isi:
- '000681815400001'
pmid:
- '34361115'
file:
- access_level: open_access
checksum: a4bc06e9a2c803ceff5a91f10b174054
content_type: application/pdf
creator: asandaue
date_created: 2021-08-16T09:35:56Z
date_updated: 2021-08-16T09:35:56Z
file_id: '9923'
file_name: 2021_InternationalJournalOfMolecularSciences_Labajová .pdf
file_size: 6132410
relation: main_file
success: 1
file_date_updated: 2021-08-16T09:35:56Z
fulldoi: https://doi.org/10.3390/ijms22158350
has_accepted_license: '1'
intvolume: ' 22'
isi: 1
issue: '15'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 2595697A-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '679239'
name: Self-Organization of the Bacterial Cell
publication: International Journal of Molecular Sciences
publication_identifier:
eissn:
- 1422-0067
issn:
- 1661-6596
publication_status: published
publisher: MDPI
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cardiolipin-containing lipid membranes attract the bacterial cell division
protein diviva
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: 22
year: '2021'
...