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Molecular and Cellular Biology, October 2004, p. 8970-8980, Vol. 24, No. 20
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.20.8970-8980.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Glycogen Synthase Kinase 3 Phosphorylates RBL2/p130 during Quiescence

Larisa Litovchick, Anton Chestukhin, and James A. DeCaprio*

Dana-Farber Cancer Institute, Boston, Massachusetts

Received 11 May 2004/ Returned for modification 9 June 2004/ Accepted 22 July 2004

Phosphorylation of the retinoblastoma-related or pocket proteins RB1/pRb, RBL1/p107, and RBL2/p130 regulates cell cycle progression and exit. While all pocket proteins are phosphorylated by cyclin-dependent kinases (CDKs) during the G1/S-phase transition, p130 is also specifically phosphorylated in G0-arrested cells. We have previously identified several phosphorylated residues that match the consensus site for glycogen synthase kinase 3 (GSK3) in the G0 form of p130. Using small-molecule inhibitors of GSK3, site-specific mutants of p130, and phospho-specific antibodies, we demonstrate here that GSK3 phosphorylates p130 during G0. Phosphorylation of p130 by GSK3 contributes to the stability of p130 but does not affect its ability to interact with E2F4 or cyclins. Regulation of p130 by GSK3 provides a novel link between growth factor signaling and regulation of the cell cycle progression and exit.

* Corresponding author. Mailing address: Dana-Farber Cancer Institute, Mayer 457, 44 Binney St., Boston, MA 02115. Phone: (617) 632-3825. Fax: (617) 632-4760. E-mail: james_decaprio{at}dfci.harvard.edu.

Molecular and Cellular Biology, October 2004, p. 8970-8980, Vol. 24, No. 20
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.20.8970-8980.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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