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Mol Cell Biol, February 1998, p. 753-761, Vol. 18, No. 2
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Functional Inactivation of the Retinoblastoma
Protein Requires Sequential Modification by at Least Two Distinct
Cyclin-cdk Complexes
Ante S.
Lundberg1,2,* and
Robert A.
Weinberg1,3
The Whitehead Institute for Biomedical
Research, Cambridge, Massachusetts 021421;
Dana-Farber Cancer Institute, Boston, Massachusetts
021152; and
Department of Biology,
Massachusetts Institute of Technology, Cambridge, Massachusetts
021393
Received 5 June 1997/Returned for modification 9 July 1997/Accepted 31 October 1997
The retinoblastoma protein (pRb) acts to constrain the
G1-S transition in mammalian cells. Phosphorylation of pRb
in G1 inactivates its growth-inhibitory function, allowing
for cell cycle progression. Although several cyclins and associated
cyclin-dependent kinases (cdks) have been implicated in pRb
phosphorylation, the precise mechanism by which pRb is phosphorylated
in vivo remains unclear. By inhibiting selectively either cdk4/6 or
cdk2, we show that endogenous D-type cyclins, acting with cdk4/6, are
able to phosphorylate pRb only partially, a process that is likely to
be completed by cyclin E-cdk2 complexes. Furthermore, cyclin E-cdk2 is
unable to phosphorylate pRb in the absence of prior phosphorylation by cyclin D-cdk4/6 complexes. Complete phosphorylation of pRb,
inactivation of E2F binding, and activation of E2F transcription occur
only after sequential action of at least two distinct G1
cyclin kinase complexes.
*
Corresponding author. Mailing address: The Whitehead
Institute for Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142. Phone: (617) 258-5176. Fax: (617) 258-5213. E-mail:
Lundberg{at}wi.mit.edu.
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