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J Biol Chem, Vol. 275, Issue 14, 10477-10483, April 7, 2000

Reciprocal Regulation via Protein-Protein Interaction between c-Myc and p21cip1/waf1/sdi1 in DNA Replication and Transcription*

Hirotake KitauraDagger , Minako ShinshiDagger , Yasuko UchikoshiDagger , Takashi OnoDagger , Toshiki Tsurimoto§, Hiroshi Yoshikawa§, Sanae M. M. Iguchi-Ariga, and Hiroyoshi ArigaDagger ||

From the Dagger  Graduate School of Pharmaceutical Sciences,  College of Medical Technology, Hokkaido University, Kita-ku, Sapporo 060-0812, Japan and § Faculty of Biological Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0101, Japan

The c-myc protooncogene product (c-Myc) is a transcription factor and is rapidly induced in resting cells following various mitogenic stimuli. c-Myc is thus suggested to play an important role in the transition from quiescence to proliferation. Despite numerous studies, including those on the connection between cyclin E/cyclin-dependent kinase 2 and c-Myc, little has been clarified about c-Myc in terms of the cell cycle regulation. Here we show that c-Myc can directly bind to the carboxyl-terminal region of the cyclin-dependent kinase inhibitor p21cip1/waf1/sdi1 and thus partially relieves the p21 of the inhibitory effect on DNA synthesis directed by the proliferating cell nuclear antigen-dependent DNA polymerase delta . As for transcription, on the other hand, the p21 binding to the Myc box II region of c-Myc blocks c-Myc-Max complex formation on the E-box and thereby suppresses the transcriptional activation from the E-box by c-Myc. These results suggest that c-Myc activates DNA replication via inactivation of p21 and that p21, vice versa, represses the transcriptional activity of c-Myc. The balance of the reciprocal inactivation between c-Myc and p21 may determine the course of cellular processes such as cell proliferation, differentiation, and apoptosis.

* This work was supported by a grant-in-aid from the Ministry of Education, Science, Culture and Sport in Japan.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: Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita 12 Nishi 6, Kita-ku, Sapporo 060-0812, Japan. Tel.: 81-11-706-3745; Fax: 81-11-706-4988; E-mail: hiro@pharm.hokudai.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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