Protein Kinase SGK Mediates Survival Signals by Phosphorylating the Forkhead Transcription Factor FKHRL1 (FOXO3a)

REFERENCES

• Alessi, D. R., F. B. Caudwell, M. Andjelkovic, B. A. Hemmings, and P. Cohen. 1996. Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase. FEBS Lett. 399:333–338.
   PubMed Web of Science ®Google Scholar
• Alessi, D. R., M. T. Kozlowski, Q. P. Weng, N. Morrice, and J. Avruch. 1998. 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr. Biol. 8:69–81.
   PubMed Web of Science ®Google Scholar
• Alliston, T. N., A. C. Maiyar, P. Buse, G. L. Firestone, and J. S. Richards. 1997. Follicle stimulating hormone-regulated expression of serum/glucocorticoid-inducible kinase in rat ovarian granulosa cells: a functional role for the Sp1 family in promoter activity. Mol. Endocrinol. 11:1934–1949.
   PubMedGoogle Scholar
• Alvarez de la Rosa, D., P. Zhang, A. Naray-Fejes-Toth, G. Fejes-Toth, and C. M. Canessa. 1999. The serum and glucocorticoid kinase sgk increases the abundance of epithelial sodium channels in the plasma membrane of Xenopus oocytes. J. Biol. Chem. 274:37834–37839.
   PubMed Web of Science ®Google Scholar
• Bellacosa, A., J. R. Testa, S. P. Staal, and P. N. Tsichlis. 1991. A retroviral oncogene, akt, encoding a serine threonine kinase containing a SH2-like region. Science 254:274–277.
   PubMed Web of Science ®Google Scholar
• Biggs, W. H. I., J. Meisenhelder, T. Hunter, W. K. Cavenee, and K. C. Arden. 1999. Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. Proc. Natl. Acad. Sci. USA 96:7421–7426.
   PubMed Web of Science ®Google Scholar
• Brunet, A., A. Bonni, M. J. Zigmond, M. Z. Lin, P. Juo, L. S. Hu, M. J. Anderson, K. C. Arden, J. Blenis, and M. E. Greenberg. 1999. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96:857–868.
   PubMed Web of Science ®Google Scholar
• Buse, P., S. H. Tran, E. Luther, P. T. Phu, G. W. Aponte, and G. L. Firestone. 1999. Cell cycle and hormonal control of nuclear-cytoplasmic localization of the serum- and glucocorticoid-inducible protein kinase, Sgk, in mammary tumor cells. A novel convergence point of anti-proliferative and proliferative cell signaling pathways. J. Biol. Chem. 274:7253–7263.
   PubMed Web of Science ®Google Scholar
• Cardone, H. M., N. Roy, H. R. Stennicke, G. S. Salvesen, T. F. Franke, E. Stanbridge, S. Frisch, and J. C. Reed. 1998. Regulation of cell death protease caspase-9 by phosphorylation. Science 282:1318–1321.
   PubMed Web of Science ®Google Scholar
• Casamayor, A., P. D. Torrance, T. Kobayashi, J. Thorner, and D. R. Alessi. 1999. Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast. Curr. Biol. 9:186–197.
   PubMed Web of Science ®Google Scholar
• Chang, H. W., M. Aoki, D. Fruman, K. R. Auger, A. Bellacosa, P. N. Tsichlis, L. C. Cantley, T. M. Roberts, and P. K. Vogt. 1997. Transformation of chicken cells by the gene encoding the catalytic subunit of PI 3-kinase. Science 276:1848–1850.
   PubMed Web of Science ®Google Scholar
• Chen, S. Y., A. Bhargava, L. Mastroberardino, O. C. Meijer, J. Wang, P. Buse, G. L. Firestone, F. Verrey, and D. Pearce. 1999. Epithelial sodium channel regulated by aldosterone-induced protein sgk. Proc. Natl. Acad. Sci. USA 96:2514–2519.
   PubMed Web of Science ®Google Scholar
• Cheng, X., Y. Ma, M. Moore, B. A. Hemmings, and S. S. Taylor. 1998. Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase. Proc. Natl. Acad. Sci. USA 95:9849–9854.
   PubMed Web of Science ®Google Scholar
• Chou, M. M., W. Hou, J. Johnson, L. K. Graham, M. H. Lee, C. S. Chen, A. C. Newton, B. S. Schaffhausen, and A. Toker. 1998. Regulation of protein kinase C zeta by PI 3-kinase and PDK-1. Curr. Biol. 8:1069–1077.
   PubMed Web of Science ®Google Scholar
• Cowling, R. T., and H. C. Birnboim. 2000. Expression of serum- and glucocorticoid-regulated kinase (sgk) mRNA is up-regulated by GM-CSF and other proinflammatory mediators in human granulocytes. J. Leukoc. Biol. 67:240–248.
   PubMed Web of Science ®Google Scholar
• Datta, S. R., A. Brunet, and M. E. Greenberg. 1999. Cellular survival: a play in three Akts. Genes Dev. 13:2905–2927.
   PubMed Web of Science ®Google Scholar
• Datta, S. R., H. Dudek, X. Tao, S. Masters, H. Fu, Y. Gotoh, and M. E. Greenberg. 1997. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91:231–241.
   PubMed Web of Science ®Google Scholar
• Datta, S. R., A. Katsov, L. Hu, A. Petros, S. W. Fesik, M. B. Yaffe, and M. E. Greenberg. 2000. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol. Cell 6:41–51.
   PubMed Web of Science ®Google Scholar
• del Peso, L., M. Gonzalez-Garcia, C. Page, R. Herrera, and G. Nunez. 1997. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278:687–689.
   PubMed Web of Science ®Google Scholar
• Downward, J.. 1998. Mechanisms and consequences of activation of protein kinase B/Akt. Curr. Opin. Cell Biol. 10:262–267.
   PubMed Web of Science ®Google Scholar
• Dudek, H., S. R. Datta, T. F. Franke, M. Birnbaum, R. Yao, G. M. Cooper, R. A. Segal, D. R. Kaplan, and M. E. Greenberg. 1997. Regulation of neuronal survival by the serine-threonine protein kinase Akt. Science 275:661–665.
   PubMed Web of Science ®Google Scholar
• Dutil, E. M., A. Toker, and A. C. Newton. 1998. Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK1). Curr. Biol. 8:1366–1375.
   PubMed Web of Science ®Google Scholar
• Guo, S., G. Rena, S. Cichy, X. He, P. Cohen, and T. Unterman. 1999. Phosphorylation of serine 256 by protein kinase B disrupts transactivation by FKHR and mediates effects of insulin on IGF binding protein-1 promoter activity through a conserved insulin response sequence. J. Biol. Chem. 274:17184–17192.
   PubMed Web of Science ®Google Scholar
• Imaizumi, K., M. Tsuda, A. Wanaka, M. Tohyama, and T. Takagi. 1994. Differential expression of sgk mRNA, a member of the Ser/Thr protein kinase gene family, in rat brain after CNS injury. Brain Res. Mol. Brain Res. 26:189–196.
   PubMedGoogle Scholar
• Jensen, C. J., M. B. Buch, T. O. Krag, B. A. Hemmings, S. Gammeltoft, and M. Frodin. 1999. 90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1. J. Biol. Chem. 274:27168–27176.
   PubMed Web of Science ®Google Scholar
• Kaestner, K. H., W. Knochel, and D. E. Martinez. 2000. Unified nomenclature for the winged helix/forkhead transcription factors. Genes Dev. 14:142–146.
   PubMed Web of Science ®Google Scholar
• Kaffman, A., N. M. Rank, and E. K. O'Shea. 1998. Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes Dev. 12:2673–2683.
   PubMed Web of Science ®Google Scholar
• Kobayashi, T., and P. Cohen. 1999. Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. Biochem. J. 339:319–328.
   PubMed Web of Science ®Google Scholar
• Komeili, A., and E. K. O'Shea. 1999. Roles of phosphorylation sites in regulating activity of the transcription factor Pho4. Science 284:977–980.
   PubMed Web of Science ®Google Scholar
• Kops, G. J., and B. M. Burgering. 1999. Forkhead transcription factors: new insights into protein kinase B (c-akt) signaling. J. Mol. Med. 77:656–665.
   PubMed Web of Science ®Google Scholar
• Kops, G. J., N. D. de Ruiter, A. M. De Vries-Smits, D. R. Powell, J. L. Bos, and B. M. Burgering. 1999. Direct control of the Forkhead transcription factor AFX by protein kinase B. Nature 398:630–634.
   PubMed Web of Science ®Google Scholar
• Le Good, J. A., W. H. Ziegler, D. B. Parekh, D. R. Alessi, P. Cohen, and P. J. Parker. 1998. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 281:2042–2045.
   PubMed Web of Science ®Google Scholar
• Lopez-Girona, A., B. Furnari, O. Mondesert, and P. Russell. 1999. Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein. Nature 397:172–175.
   PubMed Web of Science ®Google Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
   Google Scholar
• Maurer, R. A.. 1989. Both isoforms of the cAMP-dependent protein kinase catalytic subunit can activate transcription of the prolactin gene. J. Biol. Chem. 264:6870–6873.
   PubMed Web of Science ®Google Scholar
• Medema, R. H., G. J. Kops, J. L. Bos, and B. M. Burgering. 2000. AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1. Nature 404:782–787.
   PubMed Web of Science ®Google Scholar
• Nakae, J., V. Barr, and D. Accili. 2000. Differential regulation of gene expression by insulin and IGF-1 receptors correlates with phosphorylation of a single amino acid residue in the forkhead transcription factor FKHR. EMBO J. 19:989–996.
   PubMed Web of Science ®Google Scholar
• Nakae, J., B. C. Park, and D. Accili. 1999. Insulin stimulates phosphorylation of the forkhead transcription factor FKHR on serine 253 through a wortmannin-sensitive pathway. J. Biol. Chem. 274:15982–15985.
   PubMed Web of Science ®Google Scholar
• Ogg, S., S. Paradis, S. Gottlieb, G. I. Patterson, L. Lee, H. A. Tissenbaum, and G. Ruvkun. 1997. The Forkhead transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans. Nature 389:994–999.
   PubMed Web of Science ®Google Scholar
• O'Neill, E. M., A. Kaffman, E. R. Jolly, and E. K. O'Shea. 1996. Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex. Science 271:209–212.
   PubMed Web of Science ®Google Scholar
• Park, J., M. L. Leong, P. Buse, A. C. Maiyar, G. L. Firestone, and B. A. Hemmings. 1999. Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway. EMBO J. 18:3024–3033.
   PubMed Web of Science ®Google Scholar
• Pullen, N., P. B. Dennis, M. Andjelkovic, A. Dufner, S. C. Kozma, B. A. Hemmings, and G. Thomas. 1998. Phosphorylation and activation of p70s6k by PDK1. Science 279:707–710.
   PubMed Web of Science ®Google Scholar
• Rena, G., S. Guo, S. Cichy, T. G. Unterman, and P. Cohen. 1999. Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B. J. Biol. Chem. 274:17179–17183.
   PubMed Web of Science ®Google Scholar
• Richards, S. A., J. Fu, A. Romanelli, A. Shimamura, and J. Blenis. 1999. Ribosomal S6 kinase 1 (RSK1) activation requires signals dependent on and independent of the MAP kinase ERK. Curr. Biol. 9:810–820.
   PubMed Web of Science ®Google Scholar
• Takaishi, H., H. Konishi, H. Matsuzaki, Y. Ono, Y. Shirai, N. Saito, T. Kitamura, W. Ogawa, M. Kasuga, U. Kikkawa, and Y. Nishizuka. 1999. Regulation of nuclear translocation of forkhead transcription factor AFX by protein kinase B. Proc. Natl. Acad. Sci. USA 96:11836–11841.
   PubMed Web of Science ®Google Scholar
• Tang, E. D., G. Nunez, F. G. Barr, and K.-L. Guan. 1999. Negative regulation of the Forkhead transcription factor FKHR by Akt. J. Biol. Chem. 274:16741–16746.
   PubMed Web of Science ®Google Scholar
• Uberall, F., K. Hellbert, S. Kampfer, K. Maly, A. Villunger, M. Spitaler, J. Mwanjewe, G. Baier-Bitterlich, G. Baier, and H. H. Grunicke. 1999. Evidence that atypical protein kinase C-lambda and atypical protein kinase C-zeta participate in Ras-mediated reorganization of the F-actin cytoskeleton. J. Cell Biol. 144:413–425.
   PubMed Web of Science ®Google Scholar
• Vanhaesebroeck, B., and D. R. Alessi. 2000. The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J. 346:561–576.
   PubMed Web of Science ®Google Scholar
• Waldegger, S., P. Barth, G. Raber, and F. Lang. 1997. Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume. Proc. Natl. Acad. Sci. USA 94:4440–4445.
   PubMed Web of Science ®Google Scholar
• Waldegger, S., K. Klingel, P. Barth, M. Sauter, M. L. Rfer, R. Kandolf, and F. Lang. 1999. h-sgk serine-threonine protein kinase gene as transcriptional target of transforming growth factor beta in human intestine. Gastroenterology 116:1081–1088.
   PubMed Web of Science ®Google Scholar
• Webster, K. M., L. Goya, and G. L. Firestone. 1993. Immediate-early transcriptional regulation and rapid mRNA turnover of a putative serine/threonine protein kinase. J. Biol. Chem. 268:11482–11485.
   PubMed Web of Science ®Google Scholar
• Webster, K. M., L. Goya, Y. Ge, A. C. Maiyar, and G. L. Firestone. 1993. Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum. Mol. Cell. Biol. 13:2031–2040.
   PubMed Web of Science ®Google Scholar
• Xing, J., D. D. Ginty, and M. E. Greenberg. 1996. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 273:959–963.
   PubMed Web of Science ®Google Scholar