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J. Biol. Chem., Vol. 279, Issue 34, 35813-35821, August 20, 2004

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A Phosphorylation Cluster in the Chromatin-binding Region Regulates Chromosome Association of LAP2^*

Andreas Gajewski, Edina Csaszar¶, and Roland Foisner||

From the Department of Medical Biochemistry, Medical University of Vienna and the ^¶Department of Biochemistry and Molecular Cell Biology, Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, University of Vienna, A-1030 Vienna, Austria

LAP2 is a LEM family protein associated with nucleoplasmic A-type lamins and chromatin in interphase. Like lamins and other lamina proteins LAP2 is cytoplasmic in metaphase, but it associates with chromosomes prior to nuclear envelope formation in late anaphase to telophase. In vitro phosphorylation analysis and mass spectrometry identified a cluster of at least three mitotic cyclin-dependent kinase 1 phosphorylation sites in the C-terminal chromatin-binding region of LAP2 as well as four additional potential sites in the cluster, some of which were targeted alternatively in LAP2 mutated at the major sites. LAP2 mutants containing serine alanine mutations at all seven sites revealed a clear phenotype. Mutated LAP2 remained associated with chromosomes throughout mitosis, but the dissociation of lamins into the cytoplasm and nuclear envelope disassembly were not affected. These data demonstrate the in vivo significance of mitotic phosphorylation for the dynamic behavior of LAP2 in the cell cycle and show that, unlike the interaction with lamins, the chromatin association of LAP2 is regulated by multiple mitosis-specific phosphorylation at sites clustered within a defined region in the C terminus of the protein.

Received for publication, March 5, 2004 , and in revised form, June 11, 2004.

^* This study was supported by grants from the Austrian Science Research Fund (FWF, P15312), from the Jubiläumsfonds of the Austrian National Bank, and from the Österreichische Muskelforschung (to R. F.). 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.

Recipient of a fellowship from the Deutsche Forschungsgemeinschaft (DFG).

^|| To whom correspondence should be addressed: Max. F. Perutz Laboratories, University Depts. of the Vienna Biocenter, Dept. of Medical Biochemistry, Medical University of Vienna, Dr. Bohrgasse 9, A-1030 Vienna, Austria. Tel.: 43-1-4277-61680; Fax: 43-1-4277-9616; E-mail: Roland.Foisner{at}univie.ac.at.

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