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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom