Cdk4-Cyclin D1 and Cdk2-Cyclin E/A Phosphorylate Different Sites in the RB Protein

descriptionPublicationkeyboard_double_arrow_right Part of book or chapter of book , Other literature type 01 Jan 1997 English Publisher:Springer US

Authors: Yoichi Taya; Hai-Kwan Jung; Masatoshi Kitagawa; Masako Ikeda; Hideaki Higashi; Katsuyuki Tamai;

doi: 10.1007/978-1-4615-5365-6_16

Cdk4-Cyclin D1 and Cdk2-Cyclin E/A Phosphorylate Different Sites in the RB Protein

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Abstract

The growth-suppressive activity of the retinoblastoma protein (pRB) is regulated by the cell cycle-dependent phosphorylation.1–3 It has been suggested that Cdk4/6-cyclin D, Cdk2-cyclin E and Cdk2-cyclin A are successively involved in this phosphorylation at G1/S transition.2,3 However, it was not known why several different Cdks are needed and how their role is distinguished. We have now found that the consensus motif for phosphorylation by Cdk4-cyclin D1 is different from that (Ser/Thr-Pro-X-Arg/Lys) for phosphorylation by Cdk2-cyclin E/A, and that at least one site among 13–14 potential phosphorylation sites of pRB is specifically phosphorylated by Cdk4-cyclin D1 during the cell cycle.4

Related Organizations

National Cancer Research Institute
United Kingdom

10 Research products, page 1 of 1

Differential Phosphorylation of the Retinoblastoma Protein by G1/S Cyclin-dependent Kinases
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