Molecular Cell
Volume 39, Issue 1, 9 July 2010, Pages 86-99
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Article
Dephosphorylation of F-BAR Protein Cdc15 Modulates Its Conformation and Stimulates Its Scaffolding Activity at the Cell Division Site

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Summary

Cytokinesis in Schizosaccharomyces pombe requires the function of Cdc15, the founding member of the pombe cdc15 homology (PCH) family of proteins. As an early, abundant contractile ring component with multiple binding partners, Cdc15 plays a key role in organizing the ring. We demonstrate that Cdc15 phosphorylation at many sites generates a closed conformation, inhibits Cdc15 assembly at the division site in interphase, and precludes interaction of Cdc15 with its binding partners. Cdc15 dephosphorylation induces an open conformation, oligomerization, and scaffolding activity during mitosis. Cdc15 mutants with reduced phosphorylation precociously appear at the division site in filament-like structures and display increased association with protein partners and the membrane. Our results indicate that Cdc15 phosphoregulation impels both assembly and disassembly of the contractile apparatus and suggest a regulatory strategy that PCH family and BAR superfamily members might broadly employ to achieve temporal specificity in their roles as linkers between membrane and cytoskeleton.

Highlights

► Multisite phosphorylation of F-BAR protein Cdc15 inhibits its scaffolding activity ► Mitotic dephosphorylation of Cdc15 drives conformation and oligomeric state changes ► Phosphoregulation of Cdc15 controls binding to protein partners and the membrane ► Phosphosite-abolished mutant Cdc15 localizes precociously to the division site

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These authors contributed equally to this work