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A more recent version of this article appeared on October 6, 2000
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Papers In Press, published online ahead of print July 27, 2000
J. Biol. Chem, 10.1074/jbc.M004795200
Submitted on June 2, 2000
Revised on July 19, 2000
Accepted on July 26, 2000

The Amino-terminal Domain of the B Subunit of Vacuolar Hr+-ATPase Contains a Filamentous Actin Binding Site

L. Shannon Holliday, Ming Lu, Beth S. Lee, Raoul D. Nelson, Suzanne Solivan, Li Zhang, and Stephen L. Gluck

Medicine/Nephrology, University of Florida College of Medicine, Gainesville, Florida 32610

Corresponding Author: hollils{at}medicine.ufl.edu

Summary Vacuolar Hr+-ATPase (V-ATPase) binds actin filaments with high affinity (Kd = 55 nM; 1). 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's of 130 nM, and 190 nM respectively, and approached saturation at 1 mole of fusion protein per mole 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.


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