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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geprüft am 05.05.2024