期刊
FEBS LETTERS
卷 469, 期 2-3, 页码 137-141出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01265-5
关键词
V-ATPase; proton pump; enzyme regulation; acidification; vacuole; Saccharomyces cerevisiae
资金
- NIGMS NIH HHS [GM50322, R01 GM050322] Funding Source: Medline
V-ATPases consist of a complex of peripheral subunits containing catalytic sites for ATP hydrolysis, the V-1 sector, attached to several membrane subunits containing a proton pore, the V-0 sector. ATP-driven proton transport requires structural and functional coupling of the two sectors, but in vivo, the interaction between the V-1 and V-0 sectors is dynamic and is regulated by extracellular conditions. Dynamic instability appears to be a general characteristic of V-ATPases and, in yeast cells, the assembly state of V-ATPases is governed by glucose availability. The structural and functional implications of reversible disassembly of V-ATPases are discussed. (C) 2000 Federation of European Biochemical Societies.
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