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(Received for publication, October 9, 1996)
From the Cyclin-dependent kinase (Cdk) enzymes
are activated for entry into the S phase of the cell cycle. Elimination
of Cdk inhibitor protein p27Kip1 during the G1 to S
phase is required for the activation process. An inhibitor of
3-hydroxy-3-methylglutaryl-CoA reductase prevents its elimination and
leads to G1 arrest. Mevalonate and its metabolite, geranylgeranyl pyrophosphate, but not farnesyl pyrophosphate, restore
the inhibitory effect of pravastatin on the degradation of p27 and
allow Cdk2 activation. By the addition of geranylgeranyl pyrophosphate,
Rho small GTPase(s) are geranylgeranylated and translocated to
membranes during G1/S progression. The restoring effect of
geranylgeranyl pyrophosphate is abolished with botulinum C3 exoenzyme,
which specifically inactivates Rho. These results indicate (i) among
mevalonate metabolites, geranylgeranyl pyrophosphate is absolutely
required for the elimination of p27 followed by Cdk2 activation; (ii)
geranylgeranylated Rho small GTPase(s) promote the degradation of p27
during G1/S transition in FRTL-5 cells.
Volume 272, Number 1,
Issue of January 3, 1997
pp. 13-16
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
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Second Department of Internal Medicine,
Chiba University Medical School, Inohana-cho, Chuou-ku, Chiba 260, Japan, the ¶ Department of Cell Chemistry, Institute of Cellular
and Molecular Biology, Okayama University Medical School, Shikata-cho,
Okayama 700, Japan, the 
Banyu Tsukuba Research Institute in
Collaboration with Merck Research Laboratories, Okubo 3, Tsukuba
300-26, Japan, the ** Department of Internal Medicine, Chiba Municipal
Hospital, Yahagi, Chuou-ku, Chiba 260, Japan, the
Department of Pharmacology, Kyoto
University Faculty of Medicine, Yoshida, Sakyo-ku, Kyoto 606, Japan,
and the §§ Cell Regulation Section, Metabolic
Disease Branch, NIDDK, National Institutes of Health,
Bethesda, Maryland 20892
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J. Chappell, J. W. Leitner, S. Solomon, I. |
