Regulation of a third conserved phosphorylation site in SGK1.
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ABSTRACT:
SUBMITTER: Chen W
PROVIDER: S-EPMC2635031 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
Publications
Regulation of a third conserved phosphorylation site in SGK1.
Chen Wei W Chen Yue Y Xu Bing-e BE Juang Yu-Chi YC Stippec Steve S Zhao Yingming Y Cobb Melanie H MH
The Journal of biological chemistry 20081209 6
SGK1 (serum- and glucocorticoid-induced kinase 1) is a member of the AGC branch of the protein kinase family. Among well described functions of SGK1 is the regulation of epithelial transport through phosphorylation of the ubiquitin protein ligase Nedd4-2 (neuronal precursor cell expressed developmentally down-regulated 4-2). The activation of SGK1 has been widely accepted to be dependent on the phosphorylation of Thr256 in the activation loop and Ser422 in the hydrophobic motif near the C termin ...[more]
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