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Originally published In Press as doi:10.1074/jbc.M204135200 on August 8, 2002

J. Biol. Chem., Vol. 277, Issue 46, 44339-44346, November 15, 2002
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Two Distinct Domains of Protein 4.1 Critical for Assembly of Functional Nuclei in Vitro*

Sharon Wald KraussDagger §, Rebecca Heald, Gloria LeeDagger , Wataru Nunomura||, J. Aura GimmDagger , Narla MohandasDagger , and Joel Anne ChasisDagger

From the Dagger  Department of Subcellular Structure, Life Sciences Division, University of California, Lawrence Berkeley National Laboratory, Berkeley, California 94720, the  Department of Molecular and Cell Biology, Division of Cell and Developmental Biology, University of California, Berkeley, California 94720, and the || Department of Biochemistry, School of Medicine, Tokyo Women's Medical University, Shinjuku, Tokyo 162-8666, Japan

Protein 4.1R, a multifunctional structural protein, acts as an adaptor in mature red cell membrane skeletons linking spectrin-actin complexes to plasma membrane-associated proteins. In nucleated cells protein 4.1 is not associated exclusively with plasma membrane but is also detected at several important subcellular locations crucial for cell division. To identify 4.1 domains having critical functions in nuclear assembly, 4.1 domain peptides were added to Xenopus egg extract nuclear reconstitution reactions. Morphologically disorganized, replication deficient nuclei assembled when spectrin-actin-binding domain or NuMA-binding C-terminal domain peptides were present. However, control variant spectrin-actin-binding domain peptides incapable of binding actin or mutant C-terminal domain peptides with reduced NuMA binding had no deleterious effects on nuclear reconstitution. To test whether 4.1 is required for proper nuclear assembly, 4.1 isoforms were depleted with spectrin-actin binding or C-terminal domain-specific antibodies. Nuclei assembled in the depleted extracts were deranged. However, nuclear assembly could be rescued by the addition of recombinant 4.1R. Our data establish that protein 4.1 is essential for nuclear assembly and identify two distinct 4.1 domains, initially characterized in cytoskeletal interactions, that have crucial and versatile functions in nuclear assembly.

* This work was supported by National Institutes of Health Grants DK32094, DK59079 (to S. W. K.), and GM57839 (to R. H.) and funds from the Pew Scholars Program (to R. H.).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: Univ. of California, Lawrence Berkeley National Lab., 1 Cyclotron Rd., MS 74-157, Berkeley, CA 94720. Tel.: 510-486-4073; Fax: 510-486-6746; E-mail: sakrauss@lbl.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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