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J. Biol. Chem., Vol. 280, Issue 48, 39925-39933, December 2, 2005

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Dissociation of Emerin from Barrier-to-autointegration Factor Is Regulated through Mitotic Phosphorylation of Emerin in a Xenopus Egg Cell-free System^*

Yasuhiro Hirano, Masashi Segawa, Fumiko S. Ouchi¶, Yoshio Yamakawa¶, Kazuhiro Furukawa, Kunio Takeyasu, and Tsuneyoshi Horigome||1

From the Graduate School of Biostudies, Kyoto University, Kitashirakawa-ohiwakecho, Sakyo-ku, Kyoto 606-8205, the Course of Functional Biology, Graduate School of Science and Technology, Niigata University, Igarashi-2, Niigata 950-2181, the ^¶Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, and the ^||Center for Transdisciplinary Research, Niigata University, Igarashi-2, Niigata 950-2181, Japan

Emerin is the gene product of STA whose mutations cause Emery-Dreifuss muscular dystrophy. It is an inner nuclear membrane protein and phosphorylated in a cell cycle-dependent manner. However, the means of phosphorylation of emerin are poorly understood. We investigated the regulation mechanism for the binding of emerin to chromatin, focusing on its cell cycle-dependent phosphorylation in a Xenopus egg cell-free system. It was shown that emerin dissociates from chromatin depending on mitotic phosphorylation of the former, and this plays a critical role in the dissociation of emerin from barrier-to-autointegration factor (BAF). Then, we analyzed the mitotic phosphorylation sites of emerin. Emerin was strongly phosphorylated in an M-phase Xenopus egg cell-free system, and five phosphorylated sites, Ser⁴⁹, Ser⁶⁶, Thr⁶⁷, Ser¹²⁰, and Ser¹⁷⁵, were identified on analysis of chymotryptic and tryptic emerin peptides using a phosphopeptide-concentrating system coupled with a Titansphere column, which specifically binds phosphopeptides, and tandem mass spectrometry sequencing. An in vitro binding assay involving an emerin S175A point mutant protein suggested that phosphorylation at Ser¹⁷⁵ regulates the dissociation of emerin from BAF.

Received for publication, March 23, 2005 , and in revised form, September 6, 2005.

^* This work was supported by a grant-in-aid from the Ministry of Education, Science, Sports and Culture of Japan, and grants for project research from Niigata and Kyoto Universities. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 81-25-262-6160; Fax: 81-25-262-6160; E-mail: thori{at}chem.sc.niigata-u.ac.jp.

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