Affiliation:
1. Division of Nephrology, Program in Membrane Biology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts
Abstract
Phosphorylation of aquaporin-2 by PKA at serine 256 (S256) occurs in various subcellular locations during its recycling itinerary, suggesting that the protein complex necessary for AQP2 S256 phosphorylation is present in these different recycling stations. Furthermore, we showed, using PKA-null cells, that PKA activity is required for vasopressin-induced AQP2 phosphorylation. Our data reveal a complex spatial pattern of intracellular AQP2 phosphorylation at S256, shedding new light on the role of phosphorylation in AQP2 membrane accumulation.
Funder
Donald Glazer
HHS | NIH | National Institute of Diabetes and Digestive and Kidney Diseases
HHS | NIH | National Center for Research Resources
HHS | NIH | NIH Office of the Director
Publisher
American Physiological Society
Cited by
4 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献