---
_id: '14846'
abstract:
- lang: eng
  text: Contraction and flow of the actin cell cortex have emerged as a common principle
    by which cells reorganize their cytoplasm and take shape. However, how these cortical
    flows interact with adjacent cytoplasmic components, changing their form and localization,
    and how this affects cytoplasmic organization and cell shape remains unclear.
    Here we show that in ascidian oocytes, the cooperative activities of cortical
    actomyosin flows and deformation of the adjacent mitochondria-rich myoplasm drive
    oocyte cytoplasmic reorganization and shape changes following fertilization. We
    show that vegetal-directed cortical actomyosin flows, established upon oocyte
    fertilization, lead to both the accumulation of cortical actin at the vegetal
    pole of the zygote and compression and local buckling of the adjacent elastic
    solid-like myoplasm layer due to friction forces generated at their interface.
    Once cortical flows have ceased, the multiple myoplasm buckles resolve into one
    larger buckle, which again drives the formation of the contraction pole—a protuberance
    of the zygote’s vegetal pole where maternal mRNAs accumulate. Thus, our findings
    reveal a mechanism where cortical actomyosin network flows determine cytoplasmic
    reorganization and cell shape by deforming adjacent cytoplasmic components through
    friction forces.
acknowledged_ssus:
- _id: EM-Fac
- _id: Bio
- _id: NanoFab
acknowledgement: We would like to thank A. McDougall, E. Hannezo and the Heisenberg
  lab for fruitful discussions and reagents. We also thank E. Munro for the iMyo-YFP
  and Bra>iMyo-mScarlet constructs. This research was supported by the Scientific
  Service Units of the Institute of Science and Technology Austria through resources
  provided by the Electron Microscopy Facility, Imaging and Optics Facility and the
  Nanofabrication Facility. This work was supported by a Joint Project Grant from
  the FWF (I 3601-B27).
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Silvia
  full_name: Caballero Mancebo, Silvia
  id: 2F1E1758-F248-11E8-B48F-1D18A9856A87
  last_name: Caballero Mancebo
  orcid: 0000-0002-5223-3346
- first_name: Rushikesh
  full_name: Shinde, Rushikesh
  last_name: Shinde
- first_name: Madison
  full_name: Bolger-Munro, Madison
  id: 516F03FA-93A3-11EA-A7C5-D6BE3DDC885E
  last_name: Bolger-Munro
  orcid: 0000-0002-8176-4824
- first_name: Matilda
  full_name: Peruzzo, Matilda
  id: 3F920B30-F248-11E8-B48F-1D18A9856A87
  last_name: Peruzzo
  orcid: 0000-0002-3415-4628
- first_name: Gregory
  full_name: Szep, Gregory
  id: 4BFB7762-F248-11E8-B48F-1D18A9856A87
  last_name: Szep
- first_name: Irene
  full_name: Steccari, Irene
  id: 2705C766-9FE2-11EA-B224-C6773DDC885E
  last_name: Steccari
- first_name: David
  full_name: Labrousse Arias, David
  id: CD573DF4-9ED3-11E9-9D77-3223E6697425
  last_name: Labrousse Arias
- first_name: Vanessa
  full_name: Zheden, Vanessa
  id: 39C5A68A-F248-11E8-B48F-1D18A9856A87
  last_name: Zheden
  orcid: 0000-0002-9438-4783
- first_name: Jack
  full_name: Merrin, Jack
  id: 4515C308-F248-11E8-B48F-1D18A9856A87
  last_name: Merrin
  orcid: 0000-0001-5145-4609
- first_name: Andrew
  full_name: Callan-Jones, Andrew
  last_name: Callan-Jones
- first_name: Raphaël
  full_name: Voituriez, Raphaël
  last_name: Voituriez
- 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: Caballero Mancebo S, Shinde R, Bolger-Munro M, et al. Friction forces determine
    cytoplasmic reorganization and shape changes of ascidian oocytes upon fertilization.
    <i>Nature Physics</i>. 2024. doi:<a href="https://doi.org/10.1038/s41567-023-02302-1">10.1038/s41567-023-02302-1</a>
  apa: Caballero Mancebo, S., Shinde, R., Bolger-Munro, M., Peruzzo, M., Szep, G.,
    Steccari, I., … Heisenberg, C.-P. J. (2024). Friction forces determine cytoplasmic
    reorganization and shape changes of ascidian oocytes upon fertilization. <i>Nature
    Physics</i>. Springer Nature. <a href="https://doi.org/10.1038/s41567-023-02302-1">https://doi.org/10.1038/s41567-023-02302-1</a>
  chicago: Caballero Mancebo, Silvia, Rushikesh Shinde, Madison Bolger-Munro, Matilda
    Peruzzo, Gregory Szep, Irene Steccari, David Labrousse Arias, et al. “Friction
    Forces Determine Cytoplasmic Reorganization and Shape Changes of Ascidian Oocytes
    upon Fertilization.” <i>Nature Physics</i>. Springer Nature, 2024. <a href="https://doi.org/10.1038/s41567-023-02302-1">https://doi.org/10.1038/s41567-023-02302-1</a>.
  ieee: S. Caballero Mancebo <i>et al.</i>, “Friction forces determine cytoplasmic
    reorganization and shape changes of ascidian oocytes upon fertilization,” <i>Nature
    Physics</i>. Springer Nature, 2024.
  ista: Caballero Mancebo S, Shinde R, Bolger-Munro M, Peruzzo M, Szep G, Steccari
    I, Labrousse Arias D, Zheden V, Merrin J, Callan-Jones A, Voituriez R, Heisenberg
    C-PJ. 2024. Friction forces determine cytoplasmic reorganization and shape changes
    of ascidian oocytes upon fertilization. Nature Physics.
  mla: Caballero Mancebo, Silvia, et al. “Friction Forces Determine Cytoplasmic Reorganization
    and Shape Changes of Ascidian Oocytes upon Fertilization.” <i>Nature Physics</i>,
    Springer Nature, 2024, doi:<a href="https://doi.org/10.1038/s41567-023-02302-1">10.1038/s41567-023-02302-1</a>.
  short: S. Caballero Mancebo, R. Shinde, M. Bolger-Munro, M. Peruzzo, G. Szep, I.
    Steccari, D. Labrousse Arias, V. Zheden, J. Merrin, A. Callan-Jones, R. Voituriez,
    C.-P.J. Heisenberg, Nature Physics (2024).
date_created: 2024-01-21T23:00:57Z
date_published: 2024-01-09T00:00:00Z
date_updated: 2024-03-05T09:33:38Z
day: '09'
department:
- _id: CaHe
- _id: JoFi
- _id: MiSi
- _id: EM-Fac
- _id: NanoFab
doi: 10.1038/s41567-023-02302-1
has_accepted_license: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/s41567-023-02302-1
month: '01'
oa: 1
oa_version: Published Version
project:
- _id: 2646861A-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: I03601
  name: Control of embryonic cleavage pattern
publication: Nature Physics
publication_identifier:
  eissn:
  - 1745-2481
  issn:
  - 1745-2473
publication_status: epub_ahead
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - description: News on ISTA Website
    relation: press_release
    url: https://ista.ac.at/en/news/stranger-than-friction-a-force-initiating-life/
scopus_import: '1'
status: public
title: Friction forces determine cytoplasmic reorganization and shape changes of ascidian
  oocytes upon fertilization
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: '2024'
...
---
_id: '9379'
abstract:
- lang: eng
  text: When B cells encounter membrane-bound antigens, the formation and coalescence
    of B cell antigen receptor (BCR) microclusters amplifies BCR signaling. The ability
    of B cells to probe the surface of antigen-presenting cells (APCs) and respond
    to APC-bound antigens requires remodeling of the actin cytoskeleton. Initial BCR
    signaling stimulates actin-related protein (Arp) 2/3 complex-dependent actin polymerization,
    which drives B cell spreading as well as the centripetal movement and coalescence
    of BCR microclusters at the B cell-APC synapse. Sustained actin polymerization
    depends on concomitant actin filament depolymerization, which enables the recycling
    of actin monomers and Arp2/3 complexes. Cofilin-mediated severing of actin filaments
    is a rate-limiting step in the morphological changes that occur during immune
    synapse formation. Hence, regulators of cofilin activity such as WD repeat-containing
    protein 1 (Wdr1), LIM domain kinase (LIMK), and coactosin-like 1 (Cotl1) may also
    be essential for actin-dependent processes in B cells. Wdr1 enhances cofilin-mediated
    actin disassembly. Conversely, Cotl1 competes with cofilin for binding to actin
    and LIMK phosphorylates cofilin and prevents it from binding to actin filaments.
    We now show that Wdr1 and LIMK have distinct roles in BCR-induced assembly of
    the peripheral actin structures that drive B cell spreading, and that cofilin,
    Wdr1, and LIMK all contribute to the actin-dependent amplification of BCR signaling
    at the immune synapse. Depleting Cotl1 had no effect on these processes. Thus,
    the Wdr1-LIMK-cofilin axis is critical for BCR-induced actin remodeling and for
    B cell responses to APC-bound antigens.
acknowledgement: We thank the UBC Life Sciences Institute Imaging Facility andthe
  UBC Flow Cytometry Facility.
article_number: '649433'
article_processing_charge: No
article_type: original
author:
- first_name: Madison
  full_name: Bolger-Munro, Madison
  id: 516F03FA-93A3-11EA-A7C5-D6BE3DDC885E
  last_name: Bolger-Munro
  orcid: 0000-0002-8176-4824
- first_name: Kate
  full_name: Choi, Kate
  last_name: Choi
- first_name: Faith
  full_name: Cheung, Faith
  last_name: Cheung
- first_name: Yi Tian
  full_name: Liu, Yi Tian
  last_name: Liu
- first_name: May
  full_name: Dang-Lawson, May
  last_name: Dang-Lawson
- first_name: Nikola
  full_name: Deretic, Nikola
  last_name: Deretic
- first_name: Connor
  full_name: Keane, Connor
  last_name: Keane
- first_name: Michael R.
  full_name: Gold, Michael R.
  last_name: Gold
citation:
  ama: Bolger-Munro M, Choi K, Cheung F, et al. The Wdr1-LIMK-Cofilin axis controls
    B cell antigen receptor-induced actin remodeling and signaling at the immune synapse.
    <i>Frontiers in Cell and Developmental Biology</i>. 2021;9. doi:<a href="https://doi.org/10.3389/fcell.2021.649433">10.3389/fcell.2021.649433</a>
  apa: Bolger-Munro, M., Choi, K., Cheung, F., Liu, Y. T., Dang-Lawson, M., Deretic,
    N., … Gold, M. R. (2021). The Wdr1-LIMK-Cofilin axis controls B cell antigen receptor-induced
    actin remodeling and signaling at the immune synapse. <i>Frontiers in Cell and
    Developmental Biology</i>. Frontiers Media. <a href="https://doi.org/10.3389/fcell.2021.649433">https://doi.org/10.3389/fcell.2021.649433</a>
  chicago: Bolger-Munro, Madison, Kate Choi, Faith Cheung, Yi Tian Liu, May Dang-Lawson,
    Nikola Deretic, Connor Keane, and Michael R. Gold. “The Wdr1-LIMK-Cofilin Axis
    Controls B Cell Antigen Receptor-Induced Actin Remodeling and Signaling at the
    Immune Synapse.” <i>Frontiers in Cell and Developmental Biology</i>. Frontiers
    Media, 2021. <a href="https://doi.org/10.3389/fcell.2021.649433">https://doi.org/10.3389/fcell.2021.649433</a>.
  ieee: M. Bolger-Munro <i>et al.</i>, “The Wdr1-LIMK-Cofilin axis controls B cell
    antigen receptor-induced actin remodeling and signaling at the immune synapse,”
    <i>Frontiers in Cell and Developmental Biology</i>, vol. 9. Frontiers Media, 2021.
  ista: Bolger-Munro M, Choi K, Cheung F, Liu YT, Dang-Lawson M, Deretic N, Keane
    C, Gold MR. 2021. The Wdr1-LIMK-Cofilin axis controls B cell antigen receptor-induced
    actin remodeling and signaling at the immune synapse. Frontiers in Cell and Developmental
    Biology. 9, 649433.
  mla: Bolger-Munro, Madison, et al. “The Wdr1-LIMK-Cofilin Axis Controls B Cell Antigen
    Receptor-Induced Actin Remodeling and Signaling at the Immune Synapse.” <i>Frontiers
    in Cell and Developmental Biology</i>, vol. 9, 649433, Frontiers Media, 2021,
    doi:<a href="https://doi.org/10.3389/fcell.2021.649433">10.3389/fcell.2021.649433</a>.
  short: M. Bolger-Munro, K. Choi, F. Cheung, Y.T. Liu, M. Dang-Lawson, N. Deretic,
    C. Keane, M.R. Gold, Frontiers in Cell and Developmental Biology 9 (2021).
date_created: 2021-05-09T22:01:37Z
date_published: 2021-04-13T00:00:00Z
date_updated: 2023-10-18T08:19:49Z
day: '13'
ddc:
- '570'
department:
- _id: CaHe
doi: 10.3389/fcell.2021.649433
external_id:
  isi:
  - '000644419500001'
  pmid:
  - '33928084'
file:
- access_level: open_access
  checksum: 8c8a03575d2f7583f88dc3b658b0976b
  content_type: application/pdf
  creator: kschuh
  date_created: 2021-05-11T15:09:23Z
  date_updated: 2021-05-11T15:09:23Z
  file_id: '9386'
  file_name: 2021_Frontiers_Cell_Bolger-Munro.pdf
  file_size: 4076024
  relation: main_file
  success: 1
file_date_updated: 2021-05-11T15:09:23Z
has_accepted_license: '1'
intvolume: '         9'
isi: 1
keyword:
- B cell
- actin
- immune synapse
- cell spreading
- cofilin
- WDR1 (AIP1)
- LIM domain kinase
- B cell receptor (BCR)
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
pmid: 1
publication: Frontiers in Cell and Developmental Biology
publication_identifier:
  eissn:
  - 2296-634X
publication_status: published
publisher: Frontiers Media
quality_controlled: '1'
scopus_import: '1'
status: public
title: The Wdr1-LIMK-Cofilin axis controls B cell antigen receptor-induced actin remodeling
  and signaling at the immune synapse
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: 9
year: '2021'
...