| Literature DB >> 11733001 |
T Yamochi1, K Semba, K Tsuji, K Mizumoto, H Sato, Y Matsuura, I Nishimoto, M Matsuoka.
Abstract
p70ik3-1 (a 70-kDa protein) contains a cyclin box, and binds to p35cdk3 in vivo and in vitro [Matsuoka, M., Matsuura, Y., Semba, K. & Nishimoto, I. (2000) Biochem. Biophys. Res. Commun. 273, 442-447]. In spite of its structural similarity to cyclins, p70ik3-1 does not activate cyclin-dependent kinase 3 (cdk3)-mediated phosphorylation of pRb, histone H1, or the C-terminal domain of RNA polymerase II. Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation.Entities:
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Year: 2001 PMID： 11733001 DOI： 10.1046/j.0014-2956.2001.02555.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956