HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 36, 26185-26194, September 7, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/36/26185    most recent M703627200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Smardon, A. M. Articles by Kane, P. M. Search for Related Content PubMed PubMed Citation Articles by Smardon, A. M. Articles by Kane, P. M. Social Bookmarking                      What's this?

RAVE Is Essential for the Efficient Assembly of the C Subunit with the Vacuolar H⁺-ATPase^*

From the Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, New York 13210

The RAVE complex is required for stable assembly of the yeast vacuolar proton-translocating ATPase (V-ATPase) during both biosynthesis of the enzyme and regulated reassembly of disassembled V₁ and V₀ sectors. It is not yet known how RAVE effects V-ATPase assembly. Previous work has shown that V₁ peripheral or stator stalk subunits E and G are critical for binding of RAVE to cytosolic V₁ complexes, suggesting that RAVE may play a role in docking of the V₁ peripheral stalk to the V₀ complex at the membrane. Here we provide evidence for an interaction between the RAVE complex and V₁ subunit C, another subunit that has been assigned to the peripheral stalk. The C subunit is unique in that it is released from both V₁ and V₀ sectors during disassembly, suggesting that subunit C may control the regulated assembly of the V-ATPase. Mutants lacking subunit C have assembly phenotypes resembling that of RAVE mutants. Both are able to assemble V₁/V₀ complexes in vivo, but these complexes are highly unstable in vitro, and V-ATPase activity is extremely low. We show that in the absence of the RAVE complex, subunit C is not able to stably assemble with the vacuolar ATPase. Our data support a model where RAVE, through its interaction with subunit C, is facilitating V₁ peripheral stalk subunit interactions with V₀ during V-ATPase assembly.

Received for publication, May 2, 2007 , and in revised form, June 21, 2007.

^* This work was supported by a postdoctoral fellowship from the American Heart Association, New York State Affiliate (to A. M. S.) and National Institutes of Health Grant RO1 GM63742 (to P. M. K.). 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.

¹ To whom correspondence should be addressed: SUNY Upstate Medical University, 750 East Adams St., Syracuse, NY 13210. Tel.: 315-464-8742; Fax: 315-464-8750; E-mail: kanepm{at}upstate.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				H. Diab, M. Ohira, M. Liu, E. Cobb, and P. M. Kane Subunit Interactions and Requirements for Inhibition of the Yeast V1-ATPase J. Biol. Chem., May 15, 2009; 284(20): 13316 - 13325. [Abstract] [Full Text] [PDF]

				Z. Zhang, Y. Zheng, H. Mazon, E. Milgrom, N. Kitagawa, E. Kish-Trier, A. J. R. Heck, P. M. Kane, and S. Wilkens Structure of the Yeast Vacuolar ATPase J. Biol. Chem., December 19, 2008; 283(51): 35983 - 35995. [Abstract] [Full Text] [PDF]

				M. Ryan, L. A. Graham, and T. H. Stevens Voa1p Functions in V-ATPase Assembly in the Yeast Endoplasmic Reticulum Mol. Biol. Cell, December 1, 2008; 19(12): 5131 - 5142. [Abstract] [Full Text] [PDF]

				J. Qi and M. Forgac Function and Subunit Interactions of the N-terminal Domain of Subunit a (Vph1p) of the Yeast V-ATPase J. Biol. Chem., July 11, 2008; 283(28): 19274 - 19282. [Abstract] [Full Text] [PDF]

				K. Dawson, W. M. Toone, N. Jones, and C. R. M. Wilkinson Loss of Regulators of Vacuolar ATPase Function and Ceramide Synthesis Results in Multidrug Sensitivity in Schizosaccharomyces pombe Eukaryot. Cell, June 1, 2008; 7(6): 926 - 937. [Abstract] [Full Text] [PDF]

				J. Rein, M. Voss, W. Blenau, B. Walz, and O. Baumann Hormone-induced assembly and activation of V-ATPase in blowfly salivary glands is mediated by protein kinase A Am J Physiol Cell Physiol, January 1, 2008; 294(1): C56 - C65. [Abstract] [Full Text] [PDF]