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Originally published In Press as doi:10.1074/jbc.M009669200 on February 1, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16456-16463, May 11, 2001
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Mitotic Reorganization of the Intermediate Filament Protein Nestin Involves Phosphorylation by cdc2 Kinase*

Cecilia M. SahlgrenDagger §, Andrey MikhailovDagger ||, Jukka HellmanDagger , Ying-Hao Chou**, Urban LendahlDagger Dagger , Robert D. Goldman**, and John E. ErikssonDagger §§¶¶

From the Dagger  Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, P.O. Box 123, FIN-20521 Turku, Finland, the § Department of Biology, Åbo Akademi University, BioCity, FIN-20520 Turku, Finland, the || Cancer Research Center, Kashirskoe sh 24, Moscow 115478, Russia, the ** Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611, the Dagger Dagger  Department of Cell and Molecular Biology, Karolinska Institute, S-17177 Stockholm, Sweden, and the §§ Department of Biology, Laboratory of Animal Physiology, University of Turku, FIN-20014 Turku, Finland

The intermediate filament protein nestin is expressed during early stages of development in the central nervous system and in muscle tissues. Nestin expression is associated with morphologically dynamic cells, such as dividing and migrating cells. However, little is known about regulation of nestin during these cellular processes. We have characterized the phosphorylation-based regulation of nestin during different stages of the cell cycle in a neuronal progenitor cell line, ST15A. Confocal microscopy of nestin organization and 32P in vivo labeling studies show that the mitotic reorganization of nestin is accompanied by elevated phosphorylation of nestin. The phosphorylation-induced alterations in nestin organization during mitosis in ST15A cells are associated with partial disassembly of nestin filaments. Comparative in vitro and in vivo phosphorylation studies identified cdc2 as the primary mitotic kinase and Thr316 as a cdc2-specific phosphorylation site on nestin. We generated a phosphospecific nestin antibody recognizing the phosphorylated form of this site. By using this antibody we observed that nestin shows constitutive phosphorylation at Thr316, which is increased during mitosis. This study shows that nestin is reorganized during mitosis and that cdc2-mediated phosphorylation is an important regulator of nestin organization and dynamics during mitosis.

* This work was supported by the Academy of Finland (Research Council for Enviroment and Natural Resources, Grant 44191), the Erna and Victor Hasselblad Foundation, and the Jusélius Foundation.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 the Turku Graduate School of Biomedical Sciences.

¶¶ To whom correspondence should be addressed: Dept. of Biology, Laboratory of Animal Physiology, Science Bldg. 1, University of Turku, FIN-20014 Turku, Finland. Tel: 358-2-333-8036; Fax: 358-2-333-8000; E-mail: john.eriksson@utu.fi.

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