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Originally published In Press as doi:10.1074/jbc.M004795200 on July 27, 2000

J. Biol. Chem., Vol. 275, Issue 41, 32331-32337, October 13, 2000
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The Amino-terminal Domain of the B Subunit of Vacuolar H+-ATPase Contains a Filamentous Actin Binding Site*

L. Shannon HollidayDagger §, Ming LuDagger , Beth S. Lee||, Raoul D. Nelson**, Suzanne SolivanDagger , Li ZhangDagger , and Stephen L. GluckDagger §

From the Departments of Dagger  Medicine and § Anatomy & Cell Biology, University of Florida College of Medicine, Gainesville, Florida 32610, the || Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, and the ** Department of Pediatrics, University of Utah, Salt Lake City, Utah 84132

Vacuolar H+-ATPase (V-ATPase) binds actin filaments with high affinity (Kd = 55 nM; Lee, B. S., Gluck, S. L., and Holliday, L. S. (1999) J. Biol. Chem. 274, 29164-29171). We have proposed that this interaction is an important mechanism controlling transport of V-ATPase from the cytoplasm to the plasma membrane of osteoclasts. Here we show that both the B1 (kidney) and B2 (brain) isoforms of the B subunit of V-ATPase contain a microfilament binding site in their amino-terminal domain. In pelleting assays containing actin filaments and partially disrupted V-ATPase, B subunits were found in greater abundance in actin pellets than were other V-ATPase subunits, suggesting that the B subunit contained an F-actin binding site. In overlay assays, biotinylated actin filaments also bound to the B subunit. A fusion protein containing the amino-terminal half of B1 subunit bound actin filaments tightly, but fusion proteins containing the carboxyl-terminal half of B1 subunit, or the full-length E subunit, did not bind F-actin. Fusion proteins containing the amino-terminal 106 amino acids of the B1 isoform or the amino-terminal 112 amino acids of the B2 isoform bound filamentous actin with Kd values of 130 and 190 nM, respectively, and approached saturation at 1 mol of fusion protein/mol of filamentous actin. The B1 and B2 amino-terminal fusion proteins competed with V-ATPase for binding to filamentous actin. In summary, binding sites for F-actin are present in the amino-terminal domains of both isoforms of the B subunit, and likely are responsible for the interaction between V-ATPase and actin filaments in vivo.

* This work was supported by an Arthritis Investigator award from the Arthritis Foundation (to L. S. H.) and by National Institutes of Health Grants R01 DK52131 (to B. S. L.) and R01 DK38848 (to S. L. G.).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.

To whom correspondence should be addressed: Dept. of Medicine, Div. of Nephrology, 1600 Archer Rd., Campus Box 100224, University of Florida College of Medicine, Gainesville, FL 32610. Tel.: 352-392-2568; Fax: 352-392-3581; E-mail: hollils@medicine.ufl.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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