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J. Biol. Chem., Vol. 277, Issue 45, 43011-43016, November 8, 2002
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From the Xenopus actin-interacting protein 1 (XAip1) is thought to promote fragmentation of actin filaments by
cofilin. To examine the mechanism of XAip1, we measured polymer lengths
by fluorescence microscopy and the concentration of filament ends with
an elongation assay. Cofilin creates ends by severing actin filaments.
XAip1 alone does not sever actin filaments or prevent
annealing/redistribution of mechanically severed filaments and has no
effect on the concentration of ends available for subunit addition. In
the presence of XAip1, the apparent filament fragmentation by cofilin
is enhanced, but XAip1 reduces rather than increases the concentration
of ends capable of adding subunits. Electron microscopy with
gold-labeled antibodies showed that a low concentration of XAip1 bound
preferentially to one end of the filament. A high concentration of
XAip1 bound along the length of the filament. In the presence of
gelsolin-actin to cap filament barbed ends, XAip1 does not enhance
cofilin activity. We conclude that XAip1 caps the barbed end of
filaments severed by cofilin. This capping blocks annealing and
depolymerization and allows more extensive severing by cofilin.
Xenopus Actin-interacting Protein 1 (XAip1) Enhances
Cofilin Fragmentation of Filaments by Capping Filament Ends*
§,
,,¶¶
Department of Biochemistry and Molecular
Biology, Colorado State University, Fort Collins, Colorado 80523, the
§ Department of Biology, Faculty of Science, Chiba
University, Chiba 263-8522, Japan, the ¶ Structural Biology
Laboratory, The Salk Institute for Biological Studies, La Jolla,
California 92037, and the ** Department of Cell Biology,
Natural Institute for Basic Biology, Okazaki 444, Japan
*
This work was supported by grants from the National
Institutes of Health (GM35126 and GM54004 to J. R. B. and GM26338 to
T. D. P.), the Japanese Ministry of Science (to H. A.), and a
Japanese Society for Promotion of Science (JSPS) Research
Fellowship for Young Scientists (to K. O.).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.
Present address: Laboratoire de Physiologie Cellulaire
Végétale, Batiment C2, piece 435 Département de
Réponse et Dynamique Cellulaires, CEA Grenoble, 17 rue des
Martyrs, 38054 Grenoble cedex 9, France.
Present address: Dept. of Biological Chemistry, The Johns
Hopkins University School of Medicine, Baltimore, MD 21205.
§§
Present address: Dept. of Molecular, Cellular, and Developmental
Biology, Yale University, New Haven, CT 06520.
¶¶
To whom correspondence should be addressed: Dept. of
Biochemistry and Molecular Biology, Colorado State University, Fort
Collins, CO 80523-1870. Tel.: 970-491-6096; Fax: 970-491-0494; E-mail: jbamburg@lamar.colostate.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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