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J. Biol. Chem., Vol. 277, Issue 40, 37765-37770, October 4, 2002
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From the The INK4a locus on chromosome 9p21 encodes two
structurally distinct tumor suppressor proteins,
p16INK4a and the alternative reading frame protein, ARF
(p19ARF in mouse and p14ARF in human). Each of
these proteins has a role in senescence of primary cells and activates
pathways for cell cycle control and tumor suppression. The current
prevailing model proposes that p19ARF activates p53 function by
antagonizing its degradation by MDM2. It was, however, recently
shown that stabilization of p53 by p14ARF occurs independent of
the relocalization of MDM2 to the nucleolus. We have identified a novel
collaborator of ARF, CARF. It co-localizes and
interacts with ARF in the nucleolus. We demonstrate that CARF is
co-regulated with ARF, cooperates with it in activating p53, and thus
acts as a novel component of the ARF-p53-p21 pathway.
CARF Is a Novel Protein That Cooperates with Mouse
p19ARF (Human p14ARF) in Activating p53*
,,
,,§§, and
Research Center for Glycoscience,
Gene Function Research Laboratory, and ¶ Institute of
Molecular and Cell Biology, National Institute of Advanced Industrial
Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki
305-8566, Japan, the § Chugai Research Institute for Medical
Sciences, 153-2 Nagai, Niihari-mura, Ibaraki 300-4101, Japan, and the
** Children's Medical Research Institute, 214 Hawkesbury
Road, Westmead, New South Wales 2145, Australia
*
This work was supported in part by a Hougateki research
grant from the National Institute of Advanced Industrial Science and Technology (to S. C. K.).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.
Supported by a Carcinogenesis Fellowship from the New South
Wales Cancer Council.
§§
To whom correspondence should be addressed. Fax: 81-298-61- 6692;
E-mail: s-kaul@aist.go.jp.
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