The yeast V-ATPase is highly similar to V-ATPases of higher organisms and has proved to be a biochemically and genetically accessible model for many aspects of V-ATPase function. Like other V-ATPases, the yeast enzyme consists of a complex of peripheral membrane proteins, the V1 sector, attached to a complex of integral membrane subunits, the V0 sector. Multiple pathways for biosynthetic assembly of the enzyme appear to be available to cells containing a full complement of subunits and enzyme activity may be further controlled during biosynthesis by a protease activity localized to the late Golgi apparatus. Surprisingly, the assembled V-ATPase is not a static structure. Instead, fully assembled V1V0 complexes appear to exist in a dynamic equilibrium with inactive cytosolic V1 and membrane-bound V0 complexes and this equilibrium can be rapidly shifted in response to changes in carbon source. The reversible disassembly of the yeast V-ATPase may be a novel regulatory mechanism, common to V-ATPases, that works in vivo in coordination with many other regulatory mechanisms.

• PMID: 10340848
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• PubMed

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Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S. | Review

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Kane PM

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Review For