SIN-dependent phosphoinhibition of formin multimerization controls fission yeast cytokinesis
Autor: | Agnieszka P. Grzegorzewska, Craig W. Vander Kooi, David R. Kovar, Kathleen L. Gould, Alaina H. Willet, K. Adam Bohnert |
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Jazyk: | angličtina |
Rok vydání: | 2013 |
Předmět: |
Cell division
viruses macromolecular substances Schizosaccharomyces Genetics Phosphorylation Cytoskeleton Cytokinesis Sequence Deletion biology biology.organism_classification Actin cytoskeleton Cell biology Protein Structure Tertiary Actin Cytoskeleton Cytoskeletal Proteins Formins Schizosaccharomyces pombe biology.protein Schizosaccharomyces pombe Proteins Protein Multimerization Protein Kinases Developmental Biology Research Paper |
Zdroj: | Genes & Development |
Popis: | 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. |
Databáze: | OpenAIRE |
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