SIN-dependent phosphoinhibition of formin multimerization controls fission yeast cytokinesis

K. Adam Bohnert, Agnieszka P. Grzegorzewska, Alaina H. Willet, Craig W. Vander Kooi, David R. Kovar, Kathleen L. Gould

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


Many eukaryotes accomplish cell division by building and constricting a medial actomyosin-based cytokinetic ring (CR). In Schizosaccharomyces pombe, a Hippo-related signaling pathway termed the septation initiation network (SIN) controls CR formation, maintenance, and constriction. However, how the SIN regulates integral CR components was unknown. Here, we identify the essential cytokinetic formin Cdc12 as a key CR substrate of SIN kinase Sid2. Eliminating Sid2-mediated Cdc12 phosphorylation leads to persistent Cdc12 clustering, which prevents CR assembly in the absence of anillin-like Mid1 and causes CRs to collapse when cytokinesis is delayed. Molecularly, Sid2 phosphorylation of Cdc12 abrogates multimerization of a previously unrecognized Cdc12 domain that confers F-actin bundling activity. Taken together, our findings identify a SIN-triggered oligomeric switch that modulates cytokinetic formin function, revealing a novel mechanism of actin cytoskeleton regulation during cell division.

Original languageEnglish
Pages (from-to)2164-2177
Number of pages14
JournalGenes and Development
Issue number19
StatePublished - Oct 1 2013


  • Cytokinesis
  • F-actin bundling
  • Formin
  • Oligomerization
  • Phosphorylation
  • Septation initiation network

ASJC Scopus subject areas

  • General Medicine


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