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

Megan Fabbro; Bin-Bing Zhou; Mikiko Takahashi; Boris Sarcevic; Preeti Lal; Mark E Graham; Brian G Gabrielli; Phillip J Robinson; Erich A Nigg; Yoshitaka Ono; Kum Kum Khanna

doi:10.1016/j.devcel.2005.09.003

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

Dev Cell. 2005 Oct;9(4):477-88. doi: 10.1016/j.devcel.2005.09.003.

Authors

Megan Fabbro¹, Bin-Bing Zhou, Mikiko Takahashi, Boris Sarcevic, Preeti Lal, Mark E Graham, Brian G Gabrielli, Phillip J Robinson, Erich A Nigg, Yoshitaka Ono, Kum Kum Khanna

Affiliation

¹ Queensland Institute of Medical Research, P.O. Royal Brisbane Hospital, Brisbane, Queensland 4029, Australia.

PMID: 16198290
DOI: 10.1016/j.devcel.2005.09.003

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

A Kinase Anchor Proteins
Adaptor Proteins, Signal Transducing / metabolism
Amino Acid Sequence
Animals
CDC2 Protein Kinase / genetics
CDC2 Protein Kinase / metabolism*
Calmodulin-Binding Proteins / metabolism
Cell Cycle Proteins / genetics
Cell Cycle Proteins / metabolism*
Cell Division / physiology
Cell Line
Centrosome / metabolism*
Centrosome / ultrastructure
Computational Biology
Cytoskeletal Proteins / metabolism
Humans
Mitogen-Activated Protein Kinase 1 / genetics
Mitogen-Activated Protein Kinase 1 / metabolism*
Molecular Sequence Data
Nuclear Proteins / genetics
Nuclear Proteins / metabolism*
Phosphorylation
Polo-Like Kinase 1
Protein Kinases / genetics
Protein Kinases / metabolism*
Protein Serine-Threonine Kinases
Proto-Oncogene Proteins / genetics
Proto-Oncogene Proteins / metabolism*
RNA, Small Interfering / genetics
RNA, Small Interfering / metabolism
Sequence Alignment
Tissue Distribution

Substances

A Kinase Anchor Proteins
AKAP9 protein, human
Adaptor Proteins, Signal Transducing
Calmodulin-Binding Proteins
Cell Cycle Proteins
Cep55 protein, human
Cytoskeletal Proteins
Nuclear Proteins
Proto-Oncogene Proteins
RNA, Small Interfering
kendrin
Protein Kinases
Protein Serine-Threonine Kinases
CDC2 Protein Kinase
Mitogen-Activated Protein Kinase 1