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• W1994633155 abstract "Reversible assembly of the V0V1 holoenzyme from V0 and V1 subcomplexes is a widely used mechanism for regulation of vacuolar-type H+-ATPases (V-ATPases) in animal cells. In the blowfly (Calliphora vicina) salivary gland, V-ATPase is located in the apical membrane of the secretory cells and energizes the secretion of a KCl-rich saliva in response to the hormone serotonin. We have examined whether the cAMP pathway, known to be activated by serotonin, controls V-ATPase assembly and activity. Fluorescence measurements of pH changes at the luminal surface of isolated glands demonstrate that cAMP, Sp-adenosine-3',5'-cyclic monophosphorothioate, or forskolin, similar to serotonin, cause V-ATPase-dependent luminal acidification. In addition, V-ATPase-dependent ATP hydrolysis increases upon treatment with these agents. Immunofluorescence microscopy and pelleting assays have demonstrated further that V1 components become translocated from the cytoplasm to the apical membrane and V-ATPase holoenzymes are assembled at the apical membrane during conditions that increase intracellular cAMP. Because these actions occur without a change in cytosolic Ca2+, our findings suggest that the cAMP pathway mediates the reversible assembly and activation of V-ATPase molecules at the apical membrane upon hormonal stimulus." @default.
• W1994633155 created "2016-06-24" @default.
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• W1994633155 date "2006-02-28" @default.
• W1994633155 modified "2023-10-02" @default.
• W1994633155 title "cAMP regulates plasma membrane vacuolar-type H ⁺ -ATPase assembly and activity in blowfly salivary glands" @default.
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• W1994633155 doi "https://doi.org/10.1073/pnas.0600011103" @default.
• W1994633155 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1450166" @default.
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• W1994633155 hasPublicationYear "2006" @default.
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