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

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

Research output: Contribution to journalArticlepeer-review


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)
Issue number6
StatePublished - Mar 2023


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

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Developmental Biology


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