About this Biochemistry, Genetics and Molecular Biology article

Cell cycle regulatory protein p27^KIP1^ is a substrate and interacts with the protein kinase CK2 by Julio C. Tapia; Victor M. Bolanos-Garcia; Muhammed Sayed; Catherine C. Allende; Jorge E. Allende is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

## 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.

Author

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

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)