Preferences for phosphorylation sites in the retinoblastoma protein of D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro.

Abstract:

:D-type cyclin-dependent kinases (Cdk4 and Cdk6) regulate the G1 to S phase progression of the mammalian cell cycle. It has been suggested that Cdk4 and Cdk6 may have distinct functions in vivo, even though they are indistinguishable biochemically. Here we show that although these Cdks phosphorylate multiple residues in pRB, they do so with different residue selectivities in vitro; Thr821 and Thr826 are preferentially phosphorylated by Cdk6 and Cdk4, respectively. This raises the possibility different substrate specificities lead to their different roles in the regulation of cellular events. Furthermore, our results indicate the new concept that Cdk itself contributes to substrate recognition.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Takaki T,Fukasawa K,Suzuki-Takahashi I,Semba K,Kitagawa M,Taya Y,Hirai H

doi

10.1093/jb/mvi050

keywords:

subject

Has Abstract

pub_date

2005-03-01 00:00:00

pages

381-6

issue

3

eissn

0021-924X

issn

1756-2651

pii

137/3/381

journal_volume

137

pub_type

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