Actin-capping protein regulates actomyosin contractility to maintain germline architecture in C. elegans

Shinjini Ray, Priti Agarwal, Anat Nitzan, François Nédélec, Ronen Zaidel-Bar*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Actin dynamics play an important role in tissue morphogenesis, yet the control of actin filament growth takes place at the molecular level. A challenge in the field is to link the molecular function of actin regulators with their physiological function. Here, we report an in vivo role of the actin-capping protein CAP-1 in the Caenorhabditis elegans germline. We show that CAP-1 is associated with actomyosin structures in the cortex and rachis, and its depletion or overexpression led to severe structural defects in the syncytial germline and oocytes. A 60% reduction in the level of CAP-1 caused a twofold increase in F-actin and non-muscle myosin II activity, and laser incision experiments revealed an increase in rachis contractility. Cytosim simulations pointed to increased myosin as the main driver of increased contractility following loss of actin-capping protein. Double depletion of CAP-1 and myosin or Rho kinase demonstrated that the rachis architecture defects associated with CAP-1 depletion require contractility of the rachis actomyosin corset. Thus, we uncovered a physiological role for actin-capping protein in regulating actomyosin contractility to maintain reproductive tissue architecture.

Original languageEnglish
Article numberdev201099
JournalDevelopment (Cambridge)
Volume150
Issue number6
DOIs
StatePublished - Mar 2023

Funding

FundersFunder number
Edwin Munro and David Kovar
National Institutes of HealthP40 OD010440
Pan-Massachusetts Challenge
University of Chicago
Israel Science Foundation767/20
Tel Aviv University
Council for Higher Education
Mechanobiology Institute, Singapore

    Keywords

    • Actin dynamics
    • Actomyosin
    • Arp2/3 complex
    • Caenorhabditis elegans
    • Capping protein
    • Contractility
    • Cytosim
    • Cytoskeleton
    • Fertility
    • Formins
    • Morphogenesis
    • Rachis
    • Syncytial germline

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