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J. Biol. Chem., Vol. 283, Issue 13, 8462-8468, March 28, 2008

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Regulation of Nuclear Lamin Polymerization by Importin ^*

From the Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611

Nuclear lamins are integral components of the nuclear envelope and are important for the regulation of many aspects of nuclear function, including gene transcription and DNA replication. During interphase, the lamins form an intranuclear intermediate filament network that must be disassembled and reassembled when cells divide. Little is known about factors regulating this assembly/disassembly cycle. Using in vitro nuclear assembly and lamin assembly assays, we have identified a role for the nuclear transport factor importin in the regulation of lamin assembly. Exogenous importin inhibited nuclear lamin assembly in Xenopus interphase egg nuclear assembly assays. Fractionation of the egg extract used for nuclear assembly identified a high molecular weight complex containing the major egg lamin, XLB3, importin , and importin β. This complex could be dissociated by RanGTP or a competing nuclear localization sequence, indicating that lamin assembly is Ran- and importin -dependent in the egg extract. We show that the addition of importin to purified lamin B3 prevents the assembly of lamins in solution. Lamin assembly assays show that importin prevents the self-association of lamins required to assemble lamin filaments into the typical paracrystals formed in vitro. These results suggest a role for importin in regulating lamin assembly and possibly modulating the interactions of lamins with lamin-binding proteins.

Received for publication, November 26, 2007 , and in revised form, January 18, 2008.

^* This work was supported by grants from the Ellison Foundation and NCI, National Institutes of Health Grant 5RO1 CA031760–25 (to R. D. G.). 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 Both authors contributed equally to this work.

² To whom correspondence should be addressed: W129 303 E. Chicago Ave., Chicago, IL 60611. Fax: 312-503-7912; E-mail: s-adam{at}northwestern.edu.

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