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Cell cycle regulatory protein p27KIP1 is a substrate and interacts with the protein kinase CK2

✍ Scribed by Julio C. Tapia; Victor M. Bolanos-Garcia; Muhammed Sayed; Catherine C. Allende; Jorge E. Allende

Publisher: John Wiley and Sons
Year: 2004
Tongue: English
Weight: 508 KB
Volume: 91
Category: Article
ISSN: 0730-2312
DOI: 10.1002/jcb.20027

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✦ Synopsis

Abstract

The protein kinase CK2 is constituted by two catalytic (α and/or α′) and two regulatory (β) subunits. CK2 phosphorylates more than 300 proteins with important functions in the cell cycle. This study has looked at the relation between CK2 and p27^KIP1^, which is a regulator of the cell cycle and a known inhibitor of cyclin‐dependent kinases (Cdk). We demonstrated that in vitro recombinant Xenopus laevis CK2 can phosphorylate recombinant human p27^KIP1^, but this phosphorylation occurs only in the presence of the regulatory β subunit. The principal site of phosphorylation is serine‐83. Analysis using pull down and surface plasmon resonance (SPR) techniques showed that p27^KIP1^ interacts with the β subunit through two domains present in the amino and carboxyl ends, while CD spectra showed that p27^KIP1^ phosphorylation by CK2 affects its secondary structure. Altogether, these results suggest that p27^KIP1^ phosphorylation by CK2 probably involves a docking event mediated by the CK2β subunit. The phosphorylation of p27^KIP1^ by CK2 may affect its biological activity. © 2004 Wiley‐Liss, Inc.

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