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The Clp1/Cdc14 phosphatase contributes to the robustness of cytokinesis by association with anillin-related Mid1.

Clifford DM, Wolfe BA, Roberts-Galbraith RH, McDonald WH, Yates JR, Gould KL
J Cell Biol. 2008 181 (1): 79-88

PMID: 18378776 · PMCID: PMC2287289 · DOI:10.1083/jcb.200709060

Cdc14 phosphatases antagonize cyclin-dependent kinase-directed phosphorylation events and are involved in several facets of cell cycle control. We investigate the role of the fission yeast Cdc14 homologue Clp1/Flp1 in cytokinesis. We find that Clp1/Flp1 is tethered at the contractile ring (CR) through its association with anillin-related Mid1. Fluorescent recovery after photobleaching analyses indicate that Mid1, unlike other tested CR components, is anchored at the cell midzone, and this physical property is likely to account for its scaffolding role. By generating a mutation in mid1 that selectively disrupts Clp1/Flp1 tethering, we reveal the specific functional consequences of Clp1/Flp1 activity at the CR, including dephosphorylation of the essential CR component Cdc15, reductions in CR protein mobility, and CR resistance to mild perturbation. Our evidence indicates that Clp1/Flp1 must interact with the Mid1 scaffold to ensure the fidelity of Schizosaccharomyces pombe cytokinesis.

MeSH Terms (8)

Cell Cycle Proteins Cytokinesis GTP-Binding Proteins Myosins Phosphorylation Protein Tyrosine Phosphatases Schizosaccharomyces Schizosaccharomyces pombe Proteins

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