Actin Depolymerization Drives Actomyosin Ring Contraction during Budding Yeast Cytokinesis

Inês Mendes Pinto, Boris Rubinstein, Andrei Kucharavy, Jay R. Unruh, Rong Li

Research output: Contribution to journalArticlepeer-review

110 Scopus citations


Actin filaments and myosin II are evolutionarily conserved force-generating components of the contractile ring during cytokinesis. Here we show that in budding yeast, actin filament depolymerization plays a major role in actomyosin ring constriction. Cofilin mutation or chemically stabilizing actin filaments attenuate actomyosin ring constriction. Deletion of myosin II motor domain or the myosin regulatory light chain reduced the contraction rate and also the rate of actin depolymerization in the ring. We constructed a quantitative microscopic model of actomyosin ring constriction via filament sliding driven by both actin depolymerization and myosin II motor activity. Model simulations based on experimental measurements support the notion that actin depolymerization is the predominant mechanism for ring constriction. The model predicts invariability of total contraction time regardless of the initial ring size, as originally reported for C. elegans embryonic cells. This prediction was validated in yeast cells of different sizes due to different ploidies.

Original languageEnglish (US)
Pages (from-to)1247-1260
Number of pages14
JournalDevelopmental Cell
Issue number6
StatePublished - Jun 12 2012
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Developmental Biology
  • Cell Biology


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