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Published online March 31, 2008
doi:10.1083/jcb.200709060
The Journal of Cell Biology, Vol. 181, No. 1, 79-88
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Clifford et al.
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Article

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

Dawn M. Clifford1, Benjamin A. Wolfe1, Rachel H. Roberts-Galbraith1, W. Hayes McDonald2, John R. Yates, III2, and Kathleen L. Gould1

1 Howard Hughes Medical Institute and Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232
2 Department of Cell Biology, Scripps Research Institute, San Diego, CA 93037

Correspondence to Kathleen L. Gould: kathy.gould{at}vanderbilt.edu

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.

Abbreviations used in this paper: CR, contractile ring; lat A, latrunculin A; SIN, septation initiation network; TAP, tandem affinity purification; YE, yeast extract.


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