V-ATPase-energized epithelia and biological insect control.
Background is provided for the experimentally detailed contributions concerning the structure, distribution and function of V-ATPase-based ion pumps in insect epithelia. The mode of action of an insecticidal bacterial protein, which is dependent upon the V-ATPase-energized state in larval lepidopteran midgut for activity, is discussed.
Wolfersberger
M G
MG
Biology Department, Temple University, Philadelphia, PA 19122.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D004064:Digestive System / Q000378:metabolism; D004848:Epithelium / Q000378:metabolism; D007300:Insect Control; D007313:Insecta / Q000378:metabolism*; D016623:Ion Pumps / Q000502:physiology; D010572:Pest Control, Biological; D025262:Vacuolar Proton-Translocating ATPases
D016623:Ion Pumps; D000251:Adenosine Triphosphatases; D025262:Vacuolar Proton-Translocating ATPases