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J. Biol. Chem., Vol. 279, Issue 14, 14207-14212, April 2, 2004
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Microscopic Evidence That Actin-interacting Protein 1 Actively Disassembles Actin-depolymerizing Factor/Cofilin-bound Actin Filaments*
From the Department of Pathology, Emory University, Atlanta, Georgia 30322
Actin-depolymerizing factor (ADF)/cofilin and gelsolin are the two major factors to enhance actin filament disassembly. Actin-interacting protein 1 (AIP1) enhances fragmentation of ADF/cofilin-bound filaments and caps the barbed ends. However, the mechanism by which AIP1 disassembles ADF/cofilin-bound filaments is not clearly understood. Here, we directly observed the effects of these proteins on filamentous actin by fluorescence microscopy and gained novel insight into the function of ADF/cofilin and AIP1. ADF/cofilin severed filaments and AIP1 strongly enhanced disassembly at nanomolar concentrations. However, gelsolin, gelsolin-actin complex, or cytochalasin D did not enhance disassembly by ADF/cofilin, suggesting that the strong activity of AIP1 cannot be explained by simple barbed end capping. Barbed end capping by ADF/cofilin and AIP1 was weak and allowed filament elongation, whereas gelsolin or gelsolin-actin complex strongly capped and inhibited elongation. These results suggest that AIP has an active role in filament severing or depolymerization and that ADF/cofilin and AIP1 are distinct from gelsolin in modulating filament elongation.
Received for publication, December 8, 2003 , and in revised form, January 21, 2004.
* This work was supported by the National Science Foundation (Grants MCB-0110464) and the National Institute of Health (Grant R01 AR48615) (to S. O.). 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.
To whom correspondence should be addressed: Dept. of Pathology, Emory University, 615 Michael St., Whitehead Research Bldg., Rm. 105N, Atlanta, GA 30322. Tel.: 404-727-3916; Fax: 404-727-8538; E-mail: sono{at}emory.edu.
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