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J. Biol. Chem., Vol. 275, Issue 44, 34744-34749, November 3, 2000
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and 
2 Isoforms*
, and
From the Department of Molecular Biophysics and Biochemistry, Yale
University School of Medicine, New Haven, Connecticut 06520-8114
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 PP2C
2, a novel
PP2C isoform, and to PP2C
. PP2C and PP2C2 co-purified with
Mg2+-dependent Cdk2/Cdk6 phosphatase
activity in DEAE-Sepharose, Superdex-200, and Mono Q chromatographies.
Moreover, purified recombinant PP2C and PP2C2 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 PP2C and PP2C2 isoforms,
and the recombinant PP2Cs exhibited a comparable substrate preference
for a phosphothreonine containing substrate, consistent with the
conservation of threonine residues at the site of activating
phosphorylation in CDKs.
The nucleotide sequence(s) reported in this paper has been
submitted to GenBankTM/EBI Data Bank with accession number AF294792 (human PP2C2).
Current address: RCGL, National Cancer Institute, NCI-FCRDC, Bldg.
560, Office 12-91A, P.O. Box B, West 7th St., Frederick, MD
21702-1201.
§
To whom correspondence should be addressed. Tel.: 203-436-4388;
Fax: 203-432-3104; E-mail: Mark.Solomon@yale.edu.
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