Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome protein, Cep55, is required for its recruitment to midbody and cytokinesis.

Abstract:

:Centrosomes in mammalian cells have recently been implicated in cytokinesis; however, their role in this process is poorly defined. Here, we describe a human coiled-coil protein, Cep55 (centrosome protein 55 kDa), that localizes to the mother centriole during interphase. Despite its association with gamma-TuRC anchoring proteins CG-NAP and Kendrin, Cep55 is not required for microtubule nucleation. Upon mitotic entry, centrosome dissociation of Cep55 is triggered by Erk2/Cdk1-dependent phosphorylation at S425 and S428. Furthermore, Cep55 locates to the midbody and plays a role in cytokinesis, as its depletion by siRNA results in failure of this process. S425/428 phosphorylation is required for interaction with Plk1, enabling phosphorylation of Cep55 at S436. Cells expressing phosphorylation-deficient mutant forms of Cep55 undergo cytokinesis failure. These results highlight the centrosome as a site to organize phosphorylation of Cep55, enabling it to relocate to the midbody to function in mitotic exit and cytokinesis.

journal_name

Dev Cell

journal_title

Developmental cell

authors

Fabbro M,Zhou BB,Takahashi M,Sarcevic B,Lal P,Graham ME,Gabrielli BG,Robinson PJ,Nigg EA,Ono Y,Khanna KK

doi

10.1016/j.devcel.2005.09.003

keywords:

subject

Has Abstract

pub_date

2005-10-01 00:00:00

pages

477-88

issue

4

eissn

1534-5807

issn

1878-1551

pii

S1534-5807(05)00337-0

journal_volume

9

pub_type

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