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Papers In Press, published online ahead of print June 30, 2000
Dept. of Molecular Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812
Corresponding Author: hiro{at}pharm.hokudai.ac.jp
A p21Cip1/Waf1/Sdi1 is known to act as a negative cell-cycle regulator by inhibiting kinase activity of a variety of cyclin-dependent kinases. In addition to binding of the cyclin-dependent kinase to the N-terminal region of p21, p21 is also bound at its C-terminal region by PCNA, SET/TAF1 and calmodulin, indicating the versatile function of p21. In this study, we cloned cDNA encoding a novel protein named TOK-1 as a p21-C-terminal binding protein by a two-hybrid system. Two splicing isoforms of TOK-1, TOK-1a and TOK-1b, comprising 322 and 314 amino acids, respectively, were co-localized with p21 in nuclei and showed a similar expression profile to that of p21 in human tissues. TOK-1a, but not TOK-1b, directly bound to the C-terminal proximal region of p21, and both were expressed at the G1/S boundary of the cell cycle. TOK-1a also preferentially bound to an active form of cyclin-dependent kinase 2 (CDK2) via p21 and these made a ternary complex in human cells. Furthermore, the results of three different types of experiments showed that TOK-1a enhanced the inhibitory activity of p21 toward histone H1 kinase activity of CDK2. TOK-1a is thus thought to be a new type of CDK2 modulator.
J. Biol. Chem, 10.1074/jbc.M003031200
Submitted on April 10, 2000
Revised on June 20, 2000
Accepted on June 30, 2000
TOK-1, a novel p21Cip1-binding protein that cooperatively enhances p21-dependent inhibitory activity toward CDK2 kinase
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