Article
PKA regulates vacuolar H+-ATPase localization and activity via direct phosphorylation of the a subunit in kidney cells.
The Journal of biological chemistry - 6 Aug 2010
Alzamora Rodrigo, Thali Ramon F, Gong Fan, Smolak Christy, Li Hui, Baty Catherine J, Bertrand Carol A, Auchli Yolanda, Brunisholz René A, Neumann Dietbert, Hallows Kenneth R, Pastor-Soler Núria M
Abstract excerpt
The vacuolar H(+)-ATPase (V-ATPase) is a major contributor to luminal acidification in epithelia of Wolffian duct origin. In both kidney-intercalated cells and epididymal clear cells, cAMP induces V-ATPase apical membrane accumulation, which is linked to proton secretion. We have shown previously that the A subunit in the cytoplasmic V(1) sector of the V-ATPase is phosphorylated by protein kinase A (PKA). Here we...
Topics
- Amino Acid Sequence
- Animals
- Cyclic AMP-Dependent Protein Kinases
- DNA Mutational Analysis
- Gene Expression Regulation, Enzymologic
- Humans
- Kidney
- Mass Spectrometry
- Mice
- Models, Biological
- Molecular Sequence Data
- Mutation