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Regulation of the epithelial calcium channel TRPV6 by the serum and glucocorticoid‐inducible kinase isoforms SGK1 and SGK3
Author(s) -
Böhmer C.,
Palmada M.,
Kenngott C.,
Lindner R.,
Klaus F.,
Laufer J.,
Lang F.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.006
Subject(s) - sgk1 , trpv6 , pdz domain , nedd4 , microbiology and biotechnology , calcium channel , chemistry , calcium , kinase , xenopus , calcium metabolism , biology , biochemistry , gene , ubiquitin ligase , organic chemistry , ubiquitin
Epithelial calcium (re)absorption is mediated by TRPV5 and TRPV6 channels. TRPV5 is modulated by the SGK1 kinase, a process requiring the PDZ‐domain containing scaffold protein NHERF2. The present study explored whether TRPV6 is similarly regulated by SGKs and the scaffold proteins NHERF1/2. In Xenopus oocytes, SGKs activate TRPV6 by increasing its plasma membrane abundance. Deletion of the putative PDZ binding motif on TRPV6 did not abolish channel activation by SGKs. Furthermore, coexpression of neither NHERF1 nor NHERF2 affected TRPV6 or potentiated the SGKs stimulating effect. The present observations disclose a novel TRPV6 regulatory mechanism which presumably participates in calcium homeostasis.