JBC INTERFERin siRNA transfection reagent

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Volume 272, Number 34, Issue of August 22, 1997 pp. 20971-20974
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
A Unique Domain of pRb2/p130 Acts as an Inhibitor of Cdk2 Kinase Activity

(Received for publication, April 29, 1997, and in revised form, June 27, 1997)

Antonio De Luca , Timothy K. MacLachlan , Luigi Bagella , Charity Dean , Candace M. Howard , Pier Paolo Claudio , Alfonso Baldi , Kamel Khalili ** and Antonio Giordano

From the Departments of Pathology, Anatomy & Cell Biology, and Sbarro Institute for Cancer Research and Molecular Medicine, Jefferson Medical College, Philadelphia, Pennsylvania 19107 and ** Department of Biochemistry and Molecular Biology, Jefferson Institute of Molecular Medicine, Thomas Jefferson University, Philadelphia, Pennsylvania 19107

The Cdk2 kinase has long been known to be involved in the progression of mammalian cells past the G1 phase restriction point and through DNA replication in the cell cycle. The Rb family of proteins, consisting of pRb, p107, and pRb2/p130, has also been shown to monitor progression of G1 phase, mostly through their interaction with E2F family members. p107 is able to inhibit Cdk2 kinase activity through this interaction via a p21-related domain present in the C terminus of the protein. We show here that pRb2/p130 also possesses this activity, but through a separate domain. Moreover, we correlate the increased expression of pRb2/p130 during various cellular processes with the decreased kinase activity of Cdk2. We hypothesize that pRb2/p130 may act not only to bind and modify E2F activity, but also to inhibit Cdk2 kinase activity in concert with p21 in a manner different from p107.


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