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Aquaporin-2 Levelsin vitroandin vivoare Regulated by VACM-1, a Cul 5 Gene
Author(s) -
Isabelle P. Le,
Sarah K. Schultz,
Bradley T. Andresen,
Gary L. Dewey,
Ping Zhao,
Laura L. Listenberger,
Peter M.T. Deen,
Abby Buchwalter,
Christopher C. Barney,
Maria A. Burnatowska-Hledin
Publication year - 2012
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000343305
Subject(s) - aquaporin 2 , aquaporin 3 , western blot , vasopressin , biology , in vivo , chemistry , microbiology and biotechnology , medicine , aquaporin , endocrinology , gene , water channel , biochemistry , mechanical engineering , engineering , inlet
In the renal collecting duct, vasopressin regulates water permeability by a process that involves stimulation of adenylyl cyclase activity, cAMP production and subsequent translocation of water channel aquaporin-2 (AQP2) into the apical plasma membrane. We have previously shown that in cos 1 cells in vitro, both adenylyl cyclase activity and cAMP production can be regulated by VACM-1, a cul 5 gene that forms complexes involved in protein ubiquitination and subsequent degradation.

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