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- W198779102 abstract "V1V0-ATPase proton pumps are multisubunit proteins consisting of integral and peripheral subunits regulated by reversible disassembly in response to the extracellular concentration of glucose; it is hypothesized that disassembly is an energy conserving strategy to preserve ATP due to limited glucose. In the absence of glucose, the peropheral sub-complex (V1) is released into the cytoplasm and the membrane sub-complex (Vo) remains integral. The disassembled enzyme is catalytically inactive but addition of glucose to glucose-deprived cells yields reassembly of a functional holoenzyme. This project studies subunit d, a key subunit coupling ATP hydrolysis to proton transport. Subunit d remains bound to the membrane upon disassembly and interacts with different V1 and Vo subunits depending on the V-ATPase's state of assembly. We used computational models of subunit d to introduce cysteine residues that will be photo-chemically cross-linked to neighboring V-ATPase subunits using the sulfhydryl reagent MBP. This study will map subunit interactions involving subunit d in the assembled and disassembled states. It will generate new information regarding the roles of subunit d for V-ATPase function and the mechanism of glucose-dependent dissociation. Supported by NSF" @default.
- W198779102 created "2016-06-24" @default.
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- W198779102 date "2008-03-01" @default.
- W198779102 modified "2023-09-24" @default.
- W198779102 title "Studies on the Role of Subunit d for V‐ATPase Reversible Disassembly" @default.
- W198779102 doi "https://doi.org/10.1096/fasebj.22.1_supplement.630.1" @default.
- W198779102 hasPublicationYear "2008" @default.
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