Structure and regulation of insect plasma membrane H+V-ATPase

Autor(en): Wieczorek, H 
Grüber, G
Harvey, WR
Huss, M 
Merzendorfer, H 
Zeiske, W
Stichwörter: Biology; CRASSA VACUOLAR ATPASE; H+-translocating vacuolar-type ATPase; HORNWORM MANDUCA-SEXTA; Life Sciences & Biomedicine - Other Topics; MALPIGHIAN TUBULES; Manduca sexta; MESSENGER-RNA; midgut; MIDGUT EPITHELIUM; MITOCHONDRIA-RICH; PROTON PUMP; TOBACCO HORNWORM; TRANSCRIPTIONAL REGULATION; V-1 ATPase; V-1 complex; V-o complex; V-TYPE ATPASE
Erscheinungsdatum: 2000
Herausgeber: COMPANY OF BIOLOGISTS LTD
Journal: JOURNAL OF EXPERIMENTAL BIOLOGY
Volumen: 203
Ausgabe: 1
Startseite: 127
Seitenende: 135
Zusammenfassung: 
H+ V-ATPases (V-ATPases) are found in two principal locations, in endomembranes and in plasma membranes. The plasma membrane V-ATPase from the midgut of larval Manduca sexta is the sole energizer of all transepithelial secondary transport processes. At least two properties make the lepidopteran midgut a model tissue for studies of general aspects of V-ATPases. First, it is a rich source for purification of the enzyme and therefore for structural studies: 20 larvae provide up to 0.5 mg of holoenzyme, and soluble, cytosolic V-1 complexes can be obtained in even greater amounts off up to 2 mg, Second, midgut ion-tranport processes are strictly controlled by the regulation of the V-ATPase, which is the sole energizer of all ion transport in this epithelium. Recent advances in our understanding the structure of the V-1 and V-o complexes and of the regulation of the enzyme's biosynthesis and ion-transport activity will be discussed.
ISSN: 0022-0949

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