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Originally published In Press as doi:10.1074/jbc.C200292200 on May 30, 2002

J. Biol. Chem., Vol. 277, Issue 29, 25867-25869, July 19, 2002
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ACCELERATED PUBLICATION
Caveolin-associated Filamentous Actin (Cav-actin) Defines a Novel F-actin Structure in Adipocytes*

Makoto Kanzaki and Jeffrey E. PessinDagger

From the Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242-1109

Dynamic actin remodeling has been implicated in the translocation of the insulin-responsive glucose transporter 4 (GLUT4) to the plasma membrane in adipocytes. Here we show that fully differentiated 3T3L1 adipocytes have unique cortical filamentous actin structure, designated Cav-actin (caveolae-associated F-actin). During 3T3L1 adipocyte differentiation, rhodamine-phalloidin staining demonstrated the formation of a cortical actin cytoskeleton that is composed of small dot-like F-actin spikes lining the inside of the plasma membrane. Double labeling with a caveolin antibody indicated that these F-actin spikes emanate from organized rosette-like clusters of caveolae/lipid raft microdomains. In contrast, there was no obvious relationship between F-actin and caveolin localization and/or organization in 3T3L1 preadipocytes (fibroblasts). Treatments of differentiated adipocytes with latrunculin B, Clostridium difficile toxin B or a dominant-interfering TC10 mutant (TC10/T31N) disrupted the Cav-actin structure without significantly affecting the organization of clustered caveolae. Similarly, disruption of the clustered caveolae with methyl-beta -cyclodextrin also dispersed the Cav-actin structure. These data demonstrate that this novel Cav-actin structure is organized through clustered caveolae but that the formation of caveolae-rosettes are not dependent upon F-actin.

* This work was supported by National Institutes of Health research Grants DK33823 and DK59291.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.

Dagger To whom correspondence should be addressed. Tel.: 319-335-7823; Fax: 319-335-7886; E-mail: Jeffrey-Pessin@uiowa.edu.

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


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