---
_id: '14555'
abstract:
- lang: eng
  text: The intricate regulatory processes behind actin polymerization play a crucial
    role in cellular biology, including essential mechanisms such as cell migration
    or cell division. However, the self-organizing principles governing actin polymerization
    are still poorly understood. In this perspective article, we compare the Belousov-Zhabotinsky
    (BZ) reaction, a classic and well understood chemical oscillator known for its
    self-organizing spatiotemporal dynamics, with the excitable dynamics of polymerizing
    actin. While the BZ reaction originates from the domain of inorganic chemistry,
    it shares remarkable similarities with actin polymerization, including the characteristic
    propagating waves, which are influenced by geometry and external fields, and the
    emergent collective behavior. Starting with a general description of emerging
    patterns, we elaborate on single droplets or cell-level dynamics, the influence
    of geometric confinements and conclude with collective interactions. Comparing
    these two systems sheds light on the universal nature of self-organization principles
    in both living and inanimate systems.
acknowledgement: The author(s) declare that no financial support was received for
  the research, authorship, and/or publication of this article.
article_number: '1287420'
article_processing_charge: Yes
article_type: original
author:
- first_name: Michael
  full_name: Riedl, Michael
  id: 3BE60946-F248-11E8-B48F-1D18A9856A87
  last_name: Riedl
  orcid: 0000-0003-4844-6311
- first_name: Michael K
  full_name: Sixt, Michael K
  id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
  last_name: Sixt
  orcid: 0000-0002-6620-9179
citation:
  ama: Riedl M, Sixt MK. The excitable nature of polymerizing actin and the Belousov-Zhabotinsky
    reaction. <i>Frontiers in Cell and Developmental Biology</i>. 2023;11. doi:<a
    href="https://doi.org/10.3389/fcell.2023.1287420">10.3389/fcell.2023.1287420</a>
  apa: Riedl, M., &#38; Sixt, M. K. (2023). The excitable nature of polymerizing actin
    and the Belousov-Zhabotinsky reaction. <i>Frontiers in Cell and Developmental
    Biology</i>. Frontiers. <a href="https://doi.org/10.3389/fcell.2023.1287420">https://doi.org/10.3389/fcell.2023.1287420</a>
  chicago: Riedl, Michael, and Michael K Sixt. “The Excitable Nature of Polymerizing
    Actin and the Belousov-Zhabotinsky Reaction.” <i>Frontiers in Cell and Developmental
    Biology</i>. Frontiers, 2023. <a href="https://doi.org/10.3389/fcell.2023.1287420">https://doi.org/10.3389/fcell.2023.1287420</a>.
  ieee: M. Riedl and M. K. Sixt, “The excitable nature of polymerizing actin and the
    Belousov-Zhabotinsky reaction,” <i>Frontiers in Cell and Developmental Biology</i>,
    vol. 11. Frontiers, 2023.
  ista: Riedl M, Sixt MK. 2023. The excitable nature of polymerizing actin and the
    Belousov-Zhabotinsky reaction. Frontiers in Cell and Developmental Biology. 11,
    1287420.
  mla: Riedl, Michael, and Michael K. Sixt. “The Excitable Nature of Polymerizing
    Actin and the Belousov-Zhabotinsky Reaction.” <i>Frontiers in Cell and Developmental
    Biology</i>, vol. 11, 1287420, Frontiers, 2023, doi:<a href="https://doi.org/10.3389/fcell.2023.1287420">10.3389/fcell.2023.1287420</a>.
  short: M. Riedl, M.K. Sixt, Frontiers in Cell and Developmental Biology 11 (2023).
date_created: 2023-11-19T23:00:55Z
date_published: 2023-10-31T00:00:00Z
date_updated: 2023-11-20T08:44:17Z
day: '31'
ddc:
- '570'
department:
- _id: MiSi
doi: 10.3389/fcell.2023.1287420
file:
- access_level: open_access
  checksum: 61857fc3ebf019354932e7ee684658ce
  content_type: application/pdf
  creator: dernst
  date_created: 2023-11-20T08:41:15Z
  date_updated: 2023-11-20T08:41:15Z
  file_id: '14561'
  file_name: 2023_FrontiersCellDevBio_Riedl.pdf
  file_size: 2047622
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  success: 1
file_date_updated: 2023-11-20T08:41:15Z
has_accepted_license: '1'
intvolume: '        11'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
publication: Frontiers in Cell and Developmental Biology
publication_identifier:
  eissn:
  - 2296-634X
publication_status: published
publisher: Frontiers
quality_controlled: '1'
scopus_import: '1'
status: public
title: The excitable nature of polymerizing actin and the Belousov-Zhabotinsky reaction
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: 11
year: '2023'
...
---
_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'
...