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Papers In Press, published online ahead of print August 16, 2000
J. Biol. Chem, 10.1074/jbc.M006210200
Submitted on July 13, 2000
Revised on August 11, 2000
Accepted on August 16, 2000

Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta2 isoforms

Aiyang Cheng, Philipp Kaldis, and Mark J. Solomon

Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114

Corresponding Author: Mark.Solomon{at}Yale.edu

We previously reported that the activating phosphorylation on cyclin-dependent kinases in yeast (Cdc28p) and in humans (Cdk2) is removed by type 2C protein phosphatases. In this study, we characterize this PP2C-like activity in HeLa cell extract and determine that it is due to PP2Cbeta 2, a novel PP2Cbeta isoform, and to PP2Calpha . PP2Calpha and PP2Cbeta 2 co-purified with Mg2+-dependent Cdk2/Cdk6 phosphatase activity in DEAE-Sepharose, Superdex-200, and Mono Q chromatographies. Moreover, purified recombinant PP2Calpha and PP2Cbeta 2 proteins efficiently dephosphorylated monomeric Cdk2/Cdk6 in vitro. The dephosphorylation of Cdk2 and Cdk6 by PP2C isoforms was inhibited by the binding of cyclins. We found that the PP2C-like activity in HeLa cell extract, partially purified HeLa PP2Calpha and PP2Cbeta 2 isoforms, and the recombinant PP2Cs exhibited a comparable substrate preference for a phospho-threonine containing substrate, consistent with the conservation of threonine residues at the site of activating phosphorylation in CDKs.


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