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Molecular and Cellular Biology, March 2002, p. 1390-1401, Vol. 22, No. 5
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.5.1390-1401.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The B-Domain Lysine Patch of pRB Is Required for Binding to Large T Antigen and Release of E2F by Phosphorylation

Vivette D. Brown and Brenda L. Gallie*

The Ontario Cancer Institute/Princess Margaret Hospital, University Health Network, and Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5G 2M9, Canada

Received 27 September 2001/ Returned for modification 25 October 2001/ Accepted 1 November 2001

Cell cycle-dependent, site-specific phosphorylation of the retinoblastoma protein, pRB, is mediated by cyclin-dependent kinases (CDKs) and regulates the binding of pRB to many proteins. We previously showed that the interaction of pRB with E2F on DNA was regulated by the accumulation of phosphate groups on pRB. Here we show that positively charged lysine residues in the B domain of pRB are necessary for the release of pRB from E2F on DNA following phosphorylation by cyclin E-cdk2 kinase. These lysine residues are also important in the binding of the simian virus 40 large T antigen (TAg) to pRB, and mutation of these lysines to arginines alters the dependency of the pRB-TAg interaction on phosphorylation of pRB.

* Corresponding author. Mailing address: Ontario Cancer Institute/Princess Margaret Hospital, University Health Network, 610 University Ave., Toronto, Ontario M5G 2M9, Canada. Phone: (416) 946-2324. Fax: (416) 946-4619.

Molecular and Cellular Biology, March 2002, p. 1390-1401, Vol. 22, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.5.1390-1401.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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