The insect plasma membrane H+V-ATPase: Intra-, inter-, and supramolecular aspects

Autor(en): Wieczorek, H 
Huss, M 
Merzendorfer, H 
Reineke, S
Vitavska, O 
Zeiske, W
Stichwörter: actin; ACTIN CYTOSKELETON; bafilomycin; BINDING-SITE; Biophysics; Cell Biology; concanamycin; insects; K+ TRANSPORT; K+/H+ ANTIPORT; Manduca sexta; MANDUCA-SEXTA MIDGUT; midgut; POSTERIOR MIDGUT; PROTON PUMP; regulation of biosynthesis; subunit topology; TOBACCO HORNWORM MIDGUT; transepithelial K+ transport; V-ATPASE; vacuolar ATPase; YEAST VACUOLAR
Erscheinungsdatum: 2003
Herausgeber: SPRINGER/PLENUM PUBLISHERS
Journal: JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
Volumen: 35
Ausgabe: 4
Startseite: 359
Seitenende: 366
Zusammenfassung: 
The plasma membrane H+ V-ATPase from the midgut of larval Manduca sexta, commonly called the tobacco hornworm, is the sole energizer of epithelial ion transport in this tissue, being responsible for the alkalinization of the gut lumen up to a pH of more than 11 and for any active ion movement across the epithelium. This minireview deals with those topics of our recent research on this enzyme that may contribute novel aspects to the biochemistry and physiology of V-ATPases. Our research approaches include intramolecular aspects such as subunit topology and the inhibition by macrolide antibiotics, intermolecular aspects such as the hormonal regulation of V-ATPase biosynthesis and the interaction of the V-ATPase with the actin cytoskeleton, and supramolecular aspects such as the interactions of V-ATPase, K+/H+ antiporter, and ion channels, which all function as an ensemble in the transepithelial movement of potassium ions.
ISSN: 0145479X
DOI: 10.1023/A:1025733016473

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