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24 (4): 753-765

Copyright © 2005 by the European Molecular Biology Organization.

Plk1 docking to GRASP65 phosphorylated by Cdk1 suggests a mechanism for Golgi checkpoint signalling

Christian Preisinger1, Roman Körner2, Mathias Wind3,4, Wolf D Lehmann3, Robert Kopajtich1, and Francis A Barr1,+

1 Intracellular Protein Transport, Independent Junior Research Group, Max-Planck-Institute of Biochemistry, Martinsried, Germany
2 Department of Cell Biology, Max-Planck-Institute of Biochemistry, Martinsried, Germany
3 Zentrale Spektroskopie, Deutsches Krebsforschungszentrum (DKFZ), Heidelberg, Germany

Abstract: 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.

Key Words: docking • Golgi matrix • GRASP65 • polo kinase • Rab1

4 Present address: Basilea Pharmaceutica Ltd, 4005 Basel, Switzerland

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