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First published online January 16, 2009
Journal of Experimental Biology 212, 341-346 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.024067

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Review

Inhibitors of V-ATPases: old and new players

Markus Huss^* and Helmut Wieczorek

Department of Biology/Chemistry, University of Osnabrück, 49069 Osnabrück, Germany

^* Author for correspondence (e-mail: huss{at}biologie.uni-osnabrueck.de)

Accepted 29 September 2008

V-ATPases constitute a ubiquitous family of heteromultimeric, proton translocating proteins. According to their localization in a multitude of eukaryotic endomembranes and plasma membranes, they energize many different transport processes. Currently, a handful of specific inhibitors of the V-ATPase are known, which represent valuable tools for the characterization of transport processes on the level of tissues, single cells or even purified proteins. The understanding of how these inhibitors function may provide a basis to develop new drugs for the benefit of patients suffering from diseases such as osteoporosis or cancer. For this purpose, it appears absolutely essential to determine the exact inhibitor binding site in a target protein on the one side and to uncover the crucial structural elements of an inhibitor on the other side. However, even for some of the most popular and long known V-ATPase inhibitors, such as bafilomycin or concanamycin, the authentic structures of their binding sites are elusive. The aim of this review is to summarize the recent advances for the old players in the inhibition game, the plecomacrolides bafilomycin and concanamycin, and to introduce some of the new players, the macrolacton archazolid, the benzolactone enamides salicylihalamide, lobatamide, apicularen, oximidine and cruentaren, and the indolyls.

Key words: H⁺-translocating vacuolar-type ATPase, V-ATPase, antibiotic inhibitors, plecomacrolides, macrolactones, benzolactone enamides, indolyls

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