Vacuolar H+-ATPases: Intra- and intermolecular interactions

Autor(en): Huss, Markus 
Vitavska, Olga 
Albertmelcher, Andrea
Bockelmann, Svenja 
Nardmann, Christin
Tabke, Katharina 
Tiburcy, Felix 
Wieczorek, Helmut 
Stichwörter: BAFILOMYCIN/CONCANAMYCIN-BINDING-SITE; BAFILOMYCINS; Cell Biology; CROSS-LINKING; CRYSTAL-STRUCTURE; CYTOTOXIC MACROLIDES; DISSOCIATION; GLUCOSE; Interactions; STRUCTURAL ELUCIDATION; SUBUNIT-C; Transport; V-ATPases; YEAST V-ATPASE
Erscheinungsdatum: 2011
Herausgeber: ELSEVIER GMBH
Journal: EUROPEAN JOURNAL OF CELL BIOLOGY
Volumen: 90
Ausgabe: 9
Startseite: 688
Seitenende: 695
Zusammenfassung: 
V-ATPases in eukaryotes are heteromultimeric, H+-transporting proteins. They are localized in a multitude of different membranes and energize many different transport processes. Unique features of V-ATPases are, on the one hand, their ability to regulate enzymatic and ion transporting activity by the reversible dissociation of the catalytic V-1 complex from the membrane bound proton translocating V-o complex and, on the other hand, their high sensitivity to specific macrolides such as bafilomycin and concanamycin from streptomycetes or archazolid and apicularen from myxomycetes. Both features require distinct intramolecular as well as intermolecular interactions. Here we will summarize our own results together with newer developments in both of these research areas. (C) 2011 Elsevier GmbH. All rights reserved.
ISSN: 01719335
DOI: 10.1016/j.ejcb.2011.04.009

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