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GRASP65, a structural protein of the Golgi apparatus, has been linked to the sensing of Golgi structure and the integration of this information with the control of mitotic entry in the form of a Golgi checkpoint. We show that Cdk1-cyclin B is the major kinase phosphorylating GRASP65 in mitosis, and that phosphorylated GRASP65 interacts with the polo box domain of the polo-like kinase Plk1. GRASP65 is phosphorylated in its C-terminal domain at four consensus sites by Cdk1-cyclin B, and mutation of these residues to alanine essentially abolishes both mitotic phosphorylation and Plk1 binding. Expression of the wild-type GRASP65 C-terminus but not the phosphorylation defective mutant in normal rat kidney cells causes a delay but not the block in mitotic entry expected if this were a true cell cycle checkpoint. These findings identify a Plk1-dependent signalling mechanism potentially linking Golgi structure and cell cycle control, but suggest that this may not be a cell cycle checkpoint in the classical sense.

Original publication

DOI

10.1038/sj.emboj.7600569

Type

Journal article

Journal

EMBO J

Publication Date

23/02/2005

Volume

24

Pages

753 - 765

Keywords

Amino Acid Sequence, Animals, CDC2 Protein Kinase, Cell Cycle, Cell Cycle Proteins, Cell Line, Cyclin B, Golgi Apparatus, Humans, Membrane Proteins, Molecular Sequence Data, Mutation, Phosphorylation, Protein Binding, Protein Kinases, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Rats, Sequence Alignment, Signal Transduction, rab1 GTP-Binding Proteins