Structure and function of V-ATPases in endocytic and secretory organelles.
Chromaffin granules and clathrin-coated vesicles are major sources for V-ATPases of mammalian cells. Studies of these organelles have helped us to understand the structure and function of the enzyme. It was shown that V-ATPases are composed of distinct catalytic and membrane sectors containing several subunits. The subunit stoichiometry was determined to be 3A, 3B, 1C, 1D, 1E, 6c (proteolipids), 1Ac115 and ?Ac39. Additional subunits are likely to be discovered. Resolution and reconstitution of the enzyme revealed that the catalytic and membrane sectors are interdependent for their partial activity. The catalytic sector has no ATPase activity when detached from the membrane sector, and the membrane sector when depleted of the catalytic sector does not conduct protons. The mechanistic significance of these properties is discussed.
Nelson
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Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000502:physiology; D000818:Animals; D004705:Endocytosis; D008322:Mammals; D015394:Molecular Structure; D015388:Organelles / Q000201:enzymology; D011487:Protein Conformation; D025262:Vacuolar Proton-Translocating ATPases
D000251:Adenosine Triphosphatases; D025262:Vacuolar Proton-Translocating ATPases