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Originally published In Press as doi:10.1074/jbc.M205136200 on October 10, 2002

J. Biol. Chem., Vol. 277, Issue 50, 48858-48867, December 13, 2002
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Oligomerization, F-actin Interaction, and Membrane Association of the Ubiquitous Mammalian Coronin 3 Are Mediated by Its Carboxyl Terminus*

Ziqiang Spoerl, Maria Stumpf, Angelika A. NoegelDagger , and Andreas Hasse

From the Institute of Biochemistry I, Medical Faculty, University of Cologne, Joseph-Stelzmann-Strasse 52, D-50931 Köln, Germany

Coronin 3 is a ubiquitously expressed member of the coronin protein family in mammals. In fibroblasts and HEK 293 cells, it is localized both in the cytosol and in the submembranous cytoskeleton, especially at lamellipodia and membrane ruffles. The carboxyl terminus of all coronins contains a coiled coil suggested to mediate dimerization. We show here that in contrast to other coronin homologues, the recombinant human coronin 3 carboxyl terminus forms oligomers rather than dimers, and that this part is sufficient to bind to and cross-link F-actin in vitro. The carboxyl terminus alone also conferred membrane association in vivo, and removal of the coiled coil abolished membrane localization but not in vitro F-actin binding. Coronin 3 is exclusively extracted as an oligomer from both the cytosol and the membrane fraction. Because oligomerization was not reported for other coronins, it might be a key feature governing coronin 3-specific functions. Cytosolic coronin 3 showed a high degree of phosphorylation, which is likely to regulate the subcellular localization of the protein.

* 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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) W40554

Dagger To whom correspondence should be addressed. Tel.: 49-221-478-6980; Fax: 49-221-478-6979; E-mail: noegel@uni-koeln.de.

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