Protein Kinase SGK Mediates Survival Signals by Phosphorylating the Forkhead Transcription Factor FKHRL1 (FOXO3a)
By A. Brunet, Jongsun Park, Hien G. Tran, Linda S. Hu, B. Hemmings, Michael E. Greenberg. Molecular and Cellular Biology, 2001
919 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/9ccfcf1c2d491180c98e4507602e1e1b4d3efcb7
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In Cell Biology
- J. Blenis
- Lewis C. Cantley
- B. Manning
- Dervis A M Salih
- S. Schiaffino
- A. Brunet
- T. Franke
- C. Mammucari
In Molecular Biology
Citations in the corpus
- Regulation of Immune Responses by mTOR (2011, background): “Like Akt, SGK1 also phosphorylates and inhibits FOXO family members (46).”
- FoxO transcription factors in the maintenance of cellular homeostasis during aging. (2008, background): “Three of the four FoxO isoforms, FoxO1, FoxO3 and FoxO4, are crucially regulated by Akt-dependent phosphorylation at three specific sites in response to growth factor and insulin stimulation (Thr32, Ser253 and Ser315 for human FoxO3) [1-4].”
- (Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms. (2006, background): “Both SGK1 (53, 287, 384) and SGK3 (203, 372) have been shown to confer cell survival.”
- Redox regulation of FoxO transcription factors (2015, neutral): “SGK T32, (S253), S315 [314] See Akt”
- The phosphatidylinositol 3-Kinase–AKT pathway in human cancer (2002, background): “The SGK family are additional targets of PI3K that have attracted much recent attention because of their high homology to AKT and similar functional effects on survival signalling pathway”
- Sensitized RNAi screen of human kinases and phosphatases identifies new regulators of apoptosis and chemoresistance (2005, background): “Similar to Akt, SGK activation is dependent on PI(3)K activity and controls the phosphorylation and inactivation of proapoptotic proteins, such as Forkhead transcription factor”
- FOXO transcription factors at the interface between longevity and tumor suppression (2005, background): “Surprisingly, Akt and SGK preferentially phosphorylate a different combination of sites in FOXO factors (Brunet et al., 2001).”
- FoxO transcription factors; Regulation by AKT and 14-3-3 proteins. (2011, background): “Indeed, SGK was shown to phosphorylate FoxO3 on the AKT phosphorylation sites, though with different site preference than AKT: both phosphorylated the T32 site equally well, however, SGK showed preference for the S315 site andAKT for the S253 site [39].”
- AKT/PKB signaling: navigating downstream. (2007, positive): “This appears to be the case for T32 on FOXO3a, where both Akt and the closely related AGC kinase SGK can phosphorylate this site in response to PI3K-activating stimuli (Brunet et al., 2001).”