Kane P M
Department of Biochemistry and Molecular Biology, SUNY Health Science Center, Syracuse, New York 13210, USA.
J Bioenerg Biomembr. 1999 Feb;31(1):49-56. doi: 10.1023/a:1005444513542.
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.
