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

J. Biol. Chem., Vol. 282, Issue 34, 24495-24503, August 24, 2007

This Article Full Text Full Text (PDF) All Versions of this Article: 282/34/24495    most recent M702598200v1 Alert me when this article is cited 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lu, M. Articles by Gluck, S. L. Search for Related Content PubMed PubMed Citation Articles by Lu, M. Articles by Gluck, S. L. Social Bookmarking                      What's this?

Physical Interaction between Aldolase and Vacuolar H⁺-ATPase Is Essential for the Assembly and Activity of the Proton Pump^*

From the Department of Medicine, University of California School of Medicine, San Francisco, California 94143

Vacuolar proton-translocating ATPases (V-ATPases) are a family of highly conserved proton pumps that couple hydrolysis of cytosolic ATP to proton transport out of the cytosol. Although V-ATPases are involved in a number of cellular processes, how the proton pumps are regulated under physiological conditions is not well understood. We have reported that the glycolytic enzyme aldolase mediates V-ATPase assembly and activity by physical association with the proton pump (Lu, M., Holliday, L. S., Zhang, L., Dunn, W. A., and Gluck, S. L. (2001) J. Biol. Chem. 276, 30407–30413 and Lu, M., Sautin, Y., Holliday, L. S., and Gluck, S. L. (2004) J. Biol. Chem. 279, 8732–8739). In this study, we generate aldolase mutants that lack binding to the B subunit of V-ATPase but retain normal catalytic activities. Functional analysis of the aldolase mutants shows that disruption of binding between aldolase and the B subunit of V-ATPase results in disassembly and malfunction of V-ATPase. In contrast, aldolase enzymatic activity is not required for V-ATPase assembly. Taken together, these findings strongly suggest an important role for physical association between aldolase and V-ATPase in the regulation of the proton pump.

Received for publication, March 26, 2007 , and in revised form, June 1, 2007.

^* This work was supported by National Institutes of Health Grants DK64977 (to M. L.) and DK64095 (to S. L. G.). 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: University of California, San Francisco, HSE 672, Box 0532, 513 Parnassus Ave., San Francisco, CA 94143-0532. Tel.: 415-502-7996; Fax: 415-476-3381; E-mail: minglu{at}medicine.ucsf.edu.

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

This article has been cited by other articles:

				Y. Su, K. G. Blake-Palmer, S. Sorrell, B. Javid, K. Bowers, A. Zhou, S. H. Chang, S. Qamar, and F. E. Karet Human H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1 Am J Physiol Renal Physiol, October 1, 2008; 295(4): F950 - F958. [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]

				C. Gancedo and C.-L. Flores Moonlighting Proteins in Yeasts Microbiol. Mol. Biol. Rev., March 1, 2008; 72(1): 197 - 210. [Abstract] [Full Text] [PDF]