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J. Biol. Chem., Vol. 277, Issue 30, 27449-27467, July 26, 2002
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From the Cyclin G2, together with cyclin G1 and cyclin I,
defines a novel cyclin family expressed in terminally differentiated
tissues including brain and muscle. Cyclin G2 expression is
up-regulated as cells undergo cell cycle arrest or apoptosis in
response to inhibitory stimuli independent of p53 (Horne, M.,
Donaldson, K., Goolsby, G., Tran, D., Mulheisen, M., Hell, J. and Wahl,
A. (1997) J. Biol. Chem. 272, 12650-12661). We tested
the hypothesis that cyclin G2 may be a negative regulator of cell cycle
progression and found that ectopic expression of cyclin G2 induces the
formation of aberrant nuclei and cell cycle arrest in HEK293 and
Chinese hamster ovary cells. Cyclin G2 is primarily partitioned to a
detergent-resistant compartment, suggesting an association with
cytoskeletal elements. We determined that cyclin G2 and its homolog
cyclin G1 directly interact with the catalytic subunit of protein
phosphatase 2A (PP2A). An okadaic acid-sensitive (<2 nM)
phosphatase activity coprecipitates with endogenous and ectopic cyclin
G2. We found that cyclin G2 also associates with various PP2A B'
regulatory subunits, as previously shown for cyclin G1. The PP2A/A
subunit is not detectable in cyclin G2-PP2A-B'-C complexes. Notably,
cyclin G2 colocalizes with both PP2A/C and B' subunits in
detergent-resistant cellular compartments, suggesting that these
complexes form in living cells. The ability of cyclin G2 to inhibit
cell cycle progression correlates with its ability to bind PP2A/B' and
C subunits. Together, our findings suggest that cyclin G2-PP2A
complexes inhibit cell cycle progression.
Cyclin G2 Associates with Protein Phosphatase 2A Catalytic
and Regulatory B' Subunits in Active Complexes and Induces Nuclear
Aberrations and a G1/S Phase Cell Cycle Arrest*
,§,,,,,§
Department of Pharmacology, University of
Wisconsin, Madison, Wisconsin 53706-1532, the § Department
of Pharmacology, University of Iowa, Iowa City, Iowa 52242-1109, and
the ¶ Department of Biochemistry and Molecular Biology, Indiana
University, Indianapolis, Indiana 46202-5122
*
This work was supported by National Institutes of Health
Grant R01GM56900 and American Heart Association Grant 9806386X (to M. C. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: 2-530 BSB,
51 Newton Rd., Dept. of Pharmacology, University of Iowa, Iowa City, IA
52242-1109. Tel.: 319-335-8267; Fax: 319-335-8930; E-mail: mary-horne@uiowa.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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