Phosphorylation of Nedd4‐2 by Sgk1 regulates epithelial Na+ channel cell surface expression

By C. Debonneville, Sandra Y. Flores, Elena Kamynina, P. Plant, C. Tauxe, M. Thomas, Carole Münster, A. Chraïbi, J. Pratt, J. Horisberger and 3 more. EMBO Journal, 2001

723 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology, Surgery

View Paper: https://www.semanticscholar.org/paper/0a1641ec4afc1dbdbebb6ce6978a82e98dab19dc

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1. Sharad Kumar

Citations in the corpus

• (Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms. (2006, background): “In any case, SGK1 may regulate ENaC indirectly by phosphorylating the ubiquitin ligase Nedd4–2 (17, 86, 113, 243, 298, 299, 341, 386), which otherwise ubiquitinates ENaC thus preparing the channel protein for clearance from the cell membrane and subsequent degradation (302) (Fig.”
• Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure. (2002, background): “When coexpressed in Xenopus oocytes, the aldosterone-induced kinase Sgk can phosphorylate and inactivate Nedd4 leading to a retention of ENaC at the cell surface (58).”
• Physiological functions of the HECT family of ubiquitin ligases (2009, background): “Several kinases regulate ENaC, in part through NEDD4L and involving the adaptor protein 14-3-3 (Ref”