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J. Biol. Chem., Vol. 275, Issue 40, 31145-31154, October 6, 2000

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TOK-1, a Novel p21^Cip1-binding Protein That Cooperatively Enhances p21-dependent Inhibitory Activity toward CDK2 Kinase^*

Takashi Ono, Hirotake Kitaura, Hideyo Ugai^§, Takehide Murata^§, Kazunari K. Yokoyama^§, Sanae M. M. Iguchi-Ariga^¶, and Hiroyoshi Ariga^**

From the  Graduate School of Pharmaceutical Sciences, ^¶ College of Medical Technology, Hokkaido University, Kita-ku, Sapporo 060, Japan, ^§ RIKEN, Tsukuba Institute, 3-1-1 Koyadai, Tsukuba, Ibaraki, 305-0074, Japan, and  CREST, Japan Science and Technology Corp., 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan

A p21^{Cip1/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 proliferating cell nuclear antigen (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-1 and TOK-1, 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-1, but not TOK-1, directly bound to the C-terminal proximal region of p21, and both were expressed at the G₁/S boundary of the cell cycle. TOK-1 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-1 enhanced the inhibitory activity of p21 toward histone H1 kinase activity of CDK2. TOK-1 is thus thought to be a new type of CDK2 modulator.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AB040450 and AB040451.

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