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Originally published In Press as doi:10.1074/jbc.M107190200 on October 15, 2001

J. Biol. Chem., Vol. 276, Issue 51, 48526-48531, December 21, 2001
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Cell Cycle-dependent Proteolysis and Phosphorylation of Human Mcm10*

Masako IzumiDagger , Fumio YatagaiDagger §, and Fumio Hanaoka§||

From the Dagger  Division of Radioisotope Technology and § Cellular Physiology Laboratory, RIKEN (The Institute of Physical and Chemical Research), Wako, Saitama 351-0198, Japan and the  Institute for Molecular and Cellular Biology and CREST, JSTC, Osaka University, Suita, Osaka 565-0871, Japan

Mcm10 (Dna43) is an essential protein for chromosomal DNA replication in Saccharomyces cerevisiae. Recently, we identified a human Mcm10 homolog that interacts with the mammalian Orc2 and Mcm2-7 complex. We additionally demonstrated that human Mcm10 binds nuclease-resistant nuclear structures during S phase and dissociates from them in G2 phase. In this study, we have further characterized the subcellular localization, modification, and expression levels of human Mcm10 protein throughout the cell cycle. Human Mcm10 protein decreased in late M phase, remained low during G1 phase, started to accumulate, and bound chromatin at the onset of S phase. Proteasome inhibitors stabilized Mcm10 levels, suggesting that proteolysis is involved in the down-regulation of the protein in late M/G1 phase. Dissociation of Mcm10 from chromatin in G2/M phase was concomitant with alterations in the electrophoretic mobility of the protein. Treatment with lambda  phosphatase revealed that mobility shifts were due to hyperphosphorylation. These results indicate that human Mcm10 is regulated by proteolysis and phosphorylation in a cell cycle-dependent manner. It is further suggested that mammalian Mcm10 is involved in S phase progression, and not the formation of a prereplicative complex, as previously proposed from data on the S. cerevisiae protein.

* This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan and a grant from the Bioarchitect Research Project of RIKEN.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: The Inst. for Molecular and Cellular Biology, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-7975; Fax: 81-6-6877-9382; E-mail: fhanaoka@imcb.osaka-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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