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Originally published In Press as doi:10.1074/jbc.M212844200 on February 25, 2003

J. Biol. Chem., Vol. 278, Issue 20, 18499-18505, May 16, 2003
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A Novel Role for Subunit C in Mediating Binding of the H+-V-ATPase to the Actin Cytoskeleton*

Olga Vitavska, Helmut Wieczorek, and Hans MerzendorferDagger

From the Department of Biology/Chemistry, Division of Animal Physiology, University of Osnabrück, D-49069 Osnabrück, Germany

Primary proton transport by V-ATPases is regulated via the reversible dissociation of the V1V0 holoenzyme into its V1 and V0 subcomplexes. Laser scanning microscopy of different tissues from the tobacco hornworm revealed co-localization of the holoenzyme and F-actin close to the apical membranes of the epithelial cells. In midgut goblet cells, no co-localization was observed under conditions where the V1 complex detaches from the apical membrane. Binding studies, however, demonstrated that both the V1 complex and the holoenzyme interact with F-actin, the latter with an apparently higher affinity. To identify F-actin binding subunits, we performed overlay blots that revealed two V1 subunits as binding partners, namely subunit B, resembling the situation in the osteoclast V-ATPase (Holliday, L. S., Lu, M., Lee, B. S., Nelson, R. D., Solivan, S., Zhang, L., and Gluck, S. L. (2000) J. Biol. Chem. 275, 32331-32337), but, in addition, subunit C, which gets released during reversible dissociation of the holoenzyme. Overlay blots and co-pelleting assays showed that the recombinant subunit C also binds to F-actin. When the V1 complex was reconstituted with recombinant subunit C, enhanced binding to F-actin was observed. Thus, subunit C may function as an anchor protein regulating the linkage between V-ATPase and the actin-based cytoskeleton.

* This work was supported by Deutsche Forschungsgemeinschaft Grants SFB 431 and GRK 612.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) AJ519536.

Dagger To whom correspondence should be addressed. Tel.: 49-541-9693502; Fax: 49-541-9693503; E-mail: merzendorfer@biologie.uni-osnabrueck.de.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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