Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site.

Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site.
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DOI:
10.1016/j.molcel.2010.06.012
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发表时间:
2010-07-09
期刊:
影响因子:
16
通讯作者:
Gould KL
Gould KL
中科院分区:
生物学1区
文献类型:
--
作者:
Roberts-Galbraith RH;Ohi MD;Ballif BA;Chen JS;McLeod I;McDonald WH;Gygi SP;Yates JR 3rd;Gould KL

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Cytokinesis in Schizosaccharomyces pombe requires the function of Cdc15, 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.
芽殖酵母酿酒酵母中内体和肌动蛋白斑块的组装、拆卸和肌动蛋白电缆依赖性运动的活细胞成像。
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