Skip Main Navigation Links Jump to Footer

Scopus Preview

Molecular Biology of the CellVolume 30, Issue 1, 1 January 2019, Pages 96-107

The ARP2/3 complex prevents excessive formin activity during cytokinesis(Article)(Open Access)

  • Chan, F.-Y.,
  • Silva, A.M.,
  • Saramago, J.,
  • Pereira-Sousa, J.,
  • Brighton, H.E.,
  • Pereira, M.,
  • Oegema, K.,
  • Gassmann, R.,
  • Carvalho, A.X.
  • View Correspondence (jump link)
  • aInstituto de Investigação e Inovação em Saúde (i3S), Portugal
  • bInstituto de Biologia Molecular e Celular, Universidade do Porto, Porto, 4200-135, Portugal
  • cDepartment of Cellular and Molecular Medicine, Ludwig Institute for Cancer Research, University of California San Diego, San Diego, CA 92093, United States

Abstract

Cytokinesis completes cell division by constriction of an actomyosin contractile ring that separates the two daughter cells. Here we use the early Caenorhabditis elegans embryo to explore how the actin filament network in the ring and the surrounding cortex is regulated by the single cytokinesis formin CYK-1 and the ARP2/3 complex, which nucleate nonbranched and branched filaments, respectively. We show that CYK-1 and the ARP2/3 complex are the predominant F-actin nucleators responsible for generating distinct cortical F-actin architectures and that depletion of either nucleator affects the kinetics of cytokinesis. CYK-1 is critical for normal F-actin levels in the contractile ring, and acute inhibition of CYK-1 after furrow ingression slows ring constriction rate, suggesting that CYK-1 activity is required throughout ring constriction. Surprisingly, although the ARP2/3 complex does not localize in the contractile ring, depletion of the ARP2 subunit or treatment with ARP2/3 complex inhibitor delays contractile ring formation and constriction. We present evidence that the delays are due to an excess in formin-nucleated cortical F-actin, suggesting that the ARP2/3 complex negatively regulates CYK-1 activity. We conclude that the kinetics of cytokinesis are modulated by interplay between the two major actin filament nucleators. © 2019 Chan et al.

Indexed keywords

EMTREE drug terms:actin related protein 2-3 complexcell proteincyk 1 proteinF actinformin proteinmyosin adenosine triphosphataseunclassified drugactinactin related protein 2-3 complexCaenorhabditis elegans proteincyk-1 protein, C elegans
EMTREE medical terms:actin filamentArticleCaenorhabditis eleganscontrolled studycytokinesisdaughter cellembryononhumanpriority journalregulatory mechanismanimalcell polaritycytologyembryologykineticsmetabolismnonmammalian embryo
MeSH:Actin CytoskeletonActin-Related Protein 2-3 ComplexActinsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell PolarityCytokinesisEmbryo, NonmammalianKinetics

Chemicals and CAS Registry Numbers:

F actin, 39409-31-9; myosin adenosine triphosphatase;

Actin-Related Protein 2-3 Complex; Actins; Caenorhabditis elegans Proteins; cyk-1 protein, C elegans

Funding details

Funding sponsor Funding number Acronym
Fundação Portugal Telecom
ERC-2013-StG-338410-DYNEINOME,FP7/2007-2013
European Research Council
European Social FundIF/00901/2013/CP1157/ CT0001,IF/01015/2013/CP1157/CT0006
Horizon 2020640553
European Regional Development Fund
NORTE 2020
Federación Española de Enfermedades Raras

  • 1

    The research leading to these results has received funding from the European Research Council under the European Union’s Horizon 2020 research and innovation program to A.X.C. (grant agreement 640553, ACTOMYO) and under the European Union’s Seventh Framework program (FP7/2007-2013) to R.G. (grant agreement ERC-2013-StG-338410-DYNEINOME). Funding was also provided by the project Norte-01-0145-FEDER-000029–Advancing Cancer Research: From basic knowledge to application, supported by the Norte Portugal Regional Operational Programme (NORTE 2020), under the PORTUGAL 2020 Partnership Agreement, through the European Regional Development Fund (FEDER). A.X.C. and R.G. have FCT Investigator positions funded by FCT and cofunded by the European Social Fund through Programa Operacional Temático Potencial Type 4.2 promotion of scientific employment (IF/00901/2013/CP1157/ CT0001 to A.X.C. and IF/01015/2013/CP1157/CT0006 to R.G.). F.Y.C. and A.M.S. hold FCT postdoctoral fellowships SFRH/ BPD/93528/2013 and SFRH/BPD/95707/2013, respectively.

  • ISSN: 10591524
  • CODEN: MBCEE
  • Source Type: Journal
  • Original language: English
  • DOI: 10.1091/mbc.E18-07-0471
  • PubMed ID: 30403552
  • Document Type: Article
  • Publisher: American Society for Cell Biology

  Carvalho, A.X.; Instituto de Investigação e Inovação em Saúde (i3S), Portugal;
© Copyright 2019 Elsevier B.V., All rights reserved.

Cited by 1 document

Leite, J. , Osorio, D.S. , Sobral, A.F.
Network contractility during cytokinesis—from molecular to global views
(2019) Biomolecules
View details of this citation
Inform me when this document is cited in Scopus:
Set citation alert Set citation feed
{"topic":{"name":"Actins; Actin Cytoskeleton; Actin nucleation","id":22676,"uri":"Topic/22676","prominencePercentile":91.81392,"prominencePercentileString":"91.814","overallScholarlyOutput":0},"dig":"45218cf201ffd133e1a346611281dcd7ef97dea2defe35c78ae50f0e18785e03"}

SciVal Topic Prominence

Topic:
Prominence percentile: