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

Academic Article
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Overview

authors

  • Clifford, D. M.
  • Wolfe, B. A.
  • Roberts-Galbraith, R. H.
  • McDonald, W. H.
  • Yates III, John
  • Gould, K. L.

publication date

  • April 2008

journal

  • Journal of Cell Biology  Journal

abstract

  • 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.

subject areas

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

PubMed Central ID

  • PMC2287289

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200709060

PubMed ID

  • 18378776
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Additional Document Info

start page

  • 79

end page

  • 88

volume

  • 181

issue

  • 1

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