메뉴 건너뛰기




Volumn 2, Issue 10, 2001, Pages 760-768

PKB/AKT: Functional insights from genetic models

Author keywords

[No Author keywords available]

Indexed keywords

AKT1 PROTEIN, DROSOPHILA; AKT1 PROTEIN, HUMAN; DROSOPHILA PROTEIN; ONCOPROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE;

EID: 0035489468     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35096067     Document Type: Review
Times cited : (552)

References (94)
  • 1
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinostol 3-kinase
    • Franke, T. F. et al. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinostol 3-kinase. Cell 81, 727-736 (1995).
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1
  • 2
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke, T. F., Kaplan, D. R., Cantley, L. C. & Toker, A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275, 665-668 (1997).
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 3
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • Bellacosa, A., Testa, J. R., Staal, S. P. & Tsichlis, P. N. A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science 254, 274-277 (1991).
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 4
    • 0034613381 scopus 로고    scopus 로고
    • Akt/protein kinase B isoforms are differentially regulated by epidermal growth factor stimulation
    • Okano, J., Gaslightwala, I., Birnbaum, M. J., Rustgi, A. K. & Nakagawa, H. Akt/protein kinase B isoforms are differentially regulated by epidermal growth factor stimulation. J. Biol. Chem. 275, 30934-30942 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 30934-30942
    • Okano, J.1    Gaslightwala, I.2    Birnbaum, M.J.3    Rustgi, A.K.4    Nakagawa, H.5
  • 5
    • 0029804116 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase B by insulin and IGF-1
    • Alessi, D. R. et al. Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J. 15, 6541-6551 (1996). Identification of the phosphorylation mechanism of PKB/AKT activation (at Thr308 and Ser473), initiating the hunt for upstream kinases.
    • (1996) EMBO J. , vol.15 , pp. 6541-6551
    • Alessi, D.R.1
  • 6
    • 15644381754 scopus 로고    scopus 로고
    • Role of translocation in the activation and function of protein kinase B
    • Andjelkovic, M. et al. Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272, 31515-31524 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 31515-31524
    • Andjelkovic, M.1
  • 7
    • 12644301164 scopus 로고    scopus 로고
    • 3-phosphoinositide-dependent protein kinase-1 (PDK1): Structural and functional homology with the Drosophila DSTPK61 kinase
    • Alessi D. R. et al. 3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase. Curr. Biol. 7, 776-789 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 776-789
    • Alessi, D.R.1
  • 8
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha
    • Alessi D. R. et al. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha. Curr. Biol. 7, 261-269 (1997) Purification and identification of PDK-1, the T-loop kinase responsible for activating PKB/AKT. Also see reference 9.
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1
  • 9
    • 0032578999 scopus 로고    scopus 로고
    • Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B
    • Stephens, L. et al. Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. Science 279, 710-714 (1998).
    • (1998) Science , vol.279 , pp. 710-714
    • Stephens, L.1
  • 10
    • 0034607914 scopus 로고    scopus 로고
    • Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473
    • Schubert, K. M., Scheid, M. P. & Duronio, V. Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473. J. Biol. Chem. 275, 13330-13335 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 13330-13335
    • Schubert, K.M.1    Scheid, M.P.2    Duronio, V.3
  • 11
    • 0035800763 scopus 로고    scopus 로고
    • Two splice variants of protein kinase B gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site serine 472 in the carboxyl-terminal hydrophobic domain
    • Brodbeck, D., Hill, M. M. & Hemmings, B. A. Two splice variants of protein kinase B gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site serine 472 in the carboxyl-terminal hydrophobic domain. J. Biol. Chem. 276, 29550-29558 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29550-29558
    • Brodbeck, D.1    Hill, M.M.2    Hemmings, B.A.3
  • 12
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • Toker, A. & Newton, A. C. Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. J. Biol. Chem. 275, 8271-8274 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 13
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton, A. C. Regulation of protein kinase C. Curr. Opin. Cell Biol. 9, 161-167 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 14
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • Williams, M. R. et al. The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells. Curr. Biol. 10, 439-448 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 439-448
    • Williams, M.R.1
  • 15
    • 0035854677 scopus 로고    scopus 로고
    • Insulin-stimulated protein kinase B phosphorylation on Ser-473 is independent of its activity and occurs through a staurosporine-insensitive kinase
    • Hill, M. M. et al. Insulin-stimulated protein kinase B phosphorylation on Ser-473 is independent of its activity and occurs through a staurosporine-insensitive kinase. J. Biol. Chem. 276, 25643-25646 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 25643-25646
    • Hill, M.M.1
  • 16
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck, B. & Alessi, D. R. The PI3K-PDK1 connection: more than just a road to PKB. Biochem. J. 346, 561-576 (2000).
    • (2000) Biochem. J. , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 17
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of GSK-3 and PKB/AKT by the integrin linked kinase (ILK)
    • Delcommenne, M. et al. Phosphoinositide-3-OH kinase-dependent regulation of GSK-3 and PKB/AKT by the integrin linked kinase (ILK). Proc. Natl Acad. Sci. USA 95, 11211-11216 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11211-11216
    • Delcommenne, M.1
  • 18
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino acids arginine 211 and serine 343
    • Persad, S. et al. Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. J. Biol. Chem. 276, 27462-27469 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27462-27469
    • Persad, S.1
  • 19
    • 0033599029 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism
    • Lynch, D. K., Ellis, C. A., Edwards, P. A. & Miles, I. D. Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism. Oncogene 18, 8024-8032 (2000).
    • (2000) Oncogene , vol.18 , pp. 8024-8032
    • Lynch, D.K.1    Ellis, C.A.2    Edwards, P.A.3    Miles, I.D.4
  • 20
    • 0035822699 scopus 로고    scopus 로고
    • Identification of the NIMA family kinases NEK6/7 as regulators of the p70 ribosomal S6 kinase
    • Belham, C., Comb, M. J. & Avruch, J. Identification of the NIMA family kinases NEK6/7 as regulators of the p70 ribosomal S6 kinase. Curr. Biol. 11, 1155-1167 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1155-1167
    • Belham, C.1    Comb, M.J.2    Avruch, J.3
  • 21
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositide-regulated kinases: Kinase activation by phosphoinositide-dependent phosphorylation
    • Chan, T. O., Rittenhouse, S. E. & Tsichlis, P. N. AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation. Annu. Rev. Biochem. 68, 965-1014 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 965-1014
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 22
    • 0034680838 scopus 로고    scopus 로고
    • Peptide and protein library screening defines optimal substrate motifs for AKT/PKB
    • Obata, T. et al. Peptide and protein library screening defines optimal substrate motifs for AKT/PKB. J. Biol. Chem. 275, 36108-36115 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 36108-36115
    • Obata, T.1
  • 23
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M. & Hemmings, B. A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789 (1995). One of the first physiological substrates identified for PKB/AKT.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 24
    • 0030748651 scopus 로고    scopus 로고
    • Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades
    • Deprez, J., Vertommen, D., Alessi, D. R., Hue, L. & Rider, M. H. Phosphorylation and activation of heart 6-phosphofructo-2-kinase by protein kinase B and other protein kinases of the insulin signaling cascades. J. Biol. Chem. 272, 17269-17275 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 17269-17275
    • Deprez, J.1    Vertommen, D.2    Alessi, D.R.3    Hue, L.4    Rider, M.H.5
  • 25
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R. et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241 (1997).
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1
  • 26
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • Brunet, A. et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96, 857-868 (1999).
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1
  • 27
    • 0033595011 scopus 로고    scopus 로고
    • Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1
    • Biggs III, W. H., Meisenhelder, J., Hunter, T., Cavenee, W. K. & Arden, K. C. Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. Proc. Natl Acad. Sci. USA 96, 7421-7426 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7421-7426
    • Biggs III, W.H.1    Meisenhelder, J.2    Hunter, T.3    Cavenee, W.K.4    Arden, K.C.5
  • 28
    • 0033560896 scopus 로고    scopus 로고
    • Direct control of the forkhead transcription factor AFX by protein kinase B
    • Kops, G. J. et al. Direct control of the forkhead transcription factor AFX by protein kinase B. Nature 398, 630-634 (1999).
    • (1999) Nature , vol.398 , pp. 630-634
    • Kops, G.J.1
  • 29
    • 0034643331 scopus 로고    scopus 로고
    • AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1
    • Medema, R. H., Kops, G. J., Bos, J. L. & Burgering, B. M. AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1. Nature 13, 782-787 (2000).
    • (2000) Nature , vol.13 , pp. 782-787
    • Medema, R.H.1    Kops, G.J.2    Bos, J.L.3    Burgering, B.M.4
  • 30
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 beta regulates cyclin D1 proteolysis and subcellular localization
    • Diehl, J. A., Cheng, M., Roussel, M. F. & Sherr, C. J. Glycogen synthase kinase-3 beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 12, 3499-3511 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 31
    • 0034941567 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation of p21 (Cip1) regulates PCNA binding and proliferation of endothelial cells
    • Rossig, L. et al. Akt-dependent phosphorylation of p21 (Cip1) regulates PCNA binding and proliferation of endothelial cells. Mol. Cell Biol. 21, 5644-5657 (2001).
    • (2001) Mol. Cell Biol. , vol.21 , pp. 5644-5657
    • Rossig, L.1
  • 32
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • Zimmermann, S. & Moelling, K. Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 286, 1741-1744 (1999).
    • (1999) Science , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 33
    • 0033607784 scopus 로고    scopus 로고
    • Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt
    • Rommel, C. et al. Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 286, 1738-1741 (1999).
    • (1999) Science , vol.286 , pp. 1738-1741
    • Rommel, C.1
  • 34
    • 0034282892 scopus 로고    scopus 로고
    • Negative regulation of the serine/threonine kinase B-Raf by Akt
    • Guan, K. L. et al. Negative regulation of the serine/threonine kinase B-Raf by Akt. J. Biol. Chem. 275, 27354-27359 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27354-27359
    • Guan, K.L.1
  • 35
    • 0033615069 scopus 로고    scopus 로고
    • The Akt kinase signals directly to endothelial nitric oxide synthase
    • Michell, B. J. et al. The Akt kinase signals directly to endothelial nitric oxide synthase. Curr. Biol. 9, 845-848 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 845-848
    • Michell, B.J.1
  • 36
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • Dimmeler, S. et al. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature 399, 601-605 (1999).
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1
  • 37
    • 0033542414 scopus 로고    scopus 로고
    • Regulation of endothelium-derived nitric oxide production by the protein kinase Akt
    • Fulton, D. et al. Regulation of endothelium-derived nitric oxide production by the protein kinase Akt. Nature 399, 597-601 (1999).
    • (1999) Nature , vol.399 , pp. 597-601
    • Fulton, D.1
  • 38
    • 0032560521 scopus 로고    scopus 로고
    • Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signalling pathway
    • Scott, P. H., Brunn, G. J., Kohn, A. D., Roth, R. A. & Lawrence, J. C. Jr. Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signalling pathway. Proc. Natl Acad. Sci. USA 95, 7772-7777 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7772-7777
    • Scott, P.H.1    Brunn, G.J.2    Kohn, A.D.3    Roth, R.A.4    Lawrence Jr., J.C.5
  • 39
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave, B. T., Ouwens, M., Withers, D. J., Alessi, D. R. & Shepherd, P. R. Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem. J. 344, 427-431 (1999).
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 40
    • 0033527577 scopus 로고    scopus 로고
    • Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-kinase/AKT in breast cancer cells
    • Altiok, S.et al. Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-kinase/AKT in breast cancer cells. J. Biol. Chem. 274, 32274-32278 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32274-32278
    • Altiok, S.1
  • 41
    • 0033517189 scopus 로고    scopus 로고
    • NF-kappa-B activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes, O. N. et al. NF-kappa-B activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 401, 82-85 (1998).
    • (1998) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1
  • 42
    • 0033517190 scopus 로고    scopus 로고
    • NF-κB is a target of AKT in anti-apoptotic PDGF signalling
    • Romashkova, J. A. & Makarov, S. S. NF-κB is a target of AKT in anti-apoptotic PDGF signalling. Nature 401, 86-90 (1999).
    • (1999) Nature , vol.401 , pp. 86-90
    • Romashkova, J.A.1    Makarov, S.S.2
  • 43
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based profile scanning approach for genome-wide prediction of signalling pathways
    • Yaffe, M. B. et al. A motif-based profile scanning approach for genome-wide prediction of signalling pathways. Nature Biotechnol. 19, 348-353 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 348-353
    • Yaffe, M.B.1
  • 44
    • 0035368548 scopus 로고    scopus 로고
    • Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKBβ)
    • Cho, H. et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKBβ). Science 292, 1728-1731 (2001). First PKB/Akt knockout paper, demonstrating the unexpected finding of a specific role for PKBβ/Akt2 in glucose homeostasis.
    • (2001) Science , vol.292 , pp. 1728-1731
    • Cho, H.1
  • 45
    • 0035448879 scopus 로고    scopus 로고
    • Growth retardation and increased apoptosis in mice with homozygous disruption of the akt1 gene
    • Chen, W. S. et al. Growth retardation and increased apoptosis in mice with homozygous disruption of the akt1 gene. Genes Dev. 15, 2203-2208 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2203-2208
    • Chen, W.S.1
  • 46
    • 0035008874 scopus 로고    scopus 로고
    • Activation of Akt (protein kinase B) in mammary epithelium provides a critical cell survival signal required for tumor progression
    • Hutchinson, J., Jin, J., Cardiff, R. D., Woodgett, J. R. & Muller, W. J. Activation of Akt (protein kinase B) in mammary epithelium provides a critical cell survival signal required for tumor progression. Mol. Cell. Biol. 21, 2203-2212 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2203-2212
    • Hutchinson, J.1    Jin, J.2    Cardiff, R.D.3    Woodgett, J.R.4    Muller, W.J.5
  • 47
    • 0034123593 scopus 로고    scopus 로고
    • Mammary gland neoplasia: Insights from transgenic mouse models
    • Siegel, P. M., Hardy, W. R. & Muller, W. J. Mammary gland neoplasia: insights from transgenic mouse models. Bioessays 22, 554-563 (2000).
    • (2000) Bioessays , vol.22 , pp. 554-563
    • Siegel, P.M.1    Hardy, W.R.2    Muller, W.J.3
  • 48
    • 0034020459 scopus 로고    scopus 로고
    • Combined activation of Ras and Akt in neural progenitors induces glioblastoma formation in mice
    • Holland, E. C. et al. Combined activation of Ras and Akt in neural progenitors induces glioblastoma formation in mice. Nature Genet. 25, 55-57 (2000).
    • (2000) Nature Genet. , vol.25 , pp. 55-57
    • Holland, E.C.1
  • 49
    • 0028074316 scopus 로고
    • Phosphatidylinositol-3-OH kinase as a direct target of Ras
    • Rodriguez-Viciana, P. et al. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature 370, 527-532 (1994).
    • (1994) Nature , vol.370 , pp. 527-532
    • Rodriguez-Viciana, P.1
  • 50
    • 0032475861 scopus 로고    scopus 로고
    • Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
    • Stambolic, V. et al. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell 95, 29-39 (1998). First biological demonstration that PTEN negatively regulates PKB/AKT.
    • (1998) Cell , vol.95 , pp. 29-39
    • Stambolic, V.1
  • 51
    • 13144249184 scopus 로고    scopus 로고
    • High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice
    • Suzuki, A. et al. High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice. Curr. Biol. 8, 1169-1178 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1169-1178
    • Suzuki, A.1
  • 52
    • 0034658320 scopus 로고    scopus 로고
    • Protein kinase B regulates T lymphocyte survival, nuclear factor KB activation, and Bcl-X(L) levels in vivo
    • Jones, R. G. et al. Protein kinase B regulates T lymphocyte survival, nuclear factor KB activation, and Bcl-X(L) levels in vivo. J. Exp. Med. 191, 1721-1734 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1721-1734
    • Jones, R.G.1
  • 53
    • 0035399612 scopus 로고    scopus 로고
    • Expression of active protein kinase B in T cells perturbs both T and B cell homeostasis and promotes inflammation
    • Parsons, M. J. et al. Expression of active protein kinase B in T cells perturbs both T and B cell homeostasis and promotes inflammation. J. Immunol. 167, 42-48 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 42-48
    • Parsons, M.J.1
  • 55
    • 0033560707 scopus 로고    scopus 로고
    • 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
    • Kobayashi, T. & Cohen, P. 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 (1999).
    • (1999) Biochem. J. , vol.339 , pp. 319-328
    • Kobayashi, T.1    Cohen, P.2
  • 56
    • 0033151832 scopus 로고    scopus 로고
    • Serum and glucocorticoid-inducible kinase (SGK) is a target of the Pl 3-kinase-stimulated signalling pathway
    • Park, J. et al. Serum and glucocorticoid-inducible kinase (SGK) is a target of the Pl 3-kinase-stimulated signalling pathway. EMBO J. 18, 3024-3033 (1999). This report provided the first evidence that SGK is downstream of Pl3K.
    • (1999) EMBO J. , vol.18 , pp. 3024-3033
    • Park, J.1
  • 57
    • 0033602281 scopus 로고    scopus 로고
    • Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast
    • Casamayor, A., Torrance, P. D., Kobayashi, T., Thorner, J. & Alessi, D. R. Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast. Curr. Biol. 9, 186-197 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 186-197
    • Casamayor, A.1    Torrance, P.D.2    Kobayashi, T.3    Thorner, J.4    Alessi, D.R.5
  • 58
    • 0343130542 scopus 로고    scopus 로고
    • Sli2 (Ypk1), a homologue of mammalian protein kinase SGK, is a downstream kinase in the sphingolipid-mediated signaling pathway of yeast
    • Sun, Y. et al. Sli2 (Ypk1), a homologue of mammalian protein kinase SGK, is a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. Mol. Cell. Biol. 20, 4411-4419 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4411-4419
    • Sun, Y.1
  • 59
    • 0035135841 scopus 로고    scopus 로고
    • Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)
    • Brunet, A. et al. Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol. Cell. Biol. 21, 952-965 (2001). This paper provided evidence that SGK targets similar substrates to PKB/AKT.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 952-965
    • Brunet, A.1
  • 60
    • 0035943615 scopus 로고    scopus 로고
    • Serum and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf
    • Zhang, B. H. et al. Serum and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf. J. Biol. Chem. 276, 31620-31626 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 31620-31626
    • Zhang, B.H.1
  • 61
    • 0033594480 scopus 로고    scopus 로고
    • PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2
    • Balendran, A. et al. PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Curr. Biol. 9, 393-404 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 393-404
    • Balendran, A.1
  • 62
    • 0035882103 scopus 로고    scopus 로고
    • The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
    • Biondi, R. M., Kieloch, A., Currie, R. A., Deak, M. & Alessi, D. R. The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB. EMBO J. 20, 4380-4390 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4380-4390
    • Biondi, R.M.1    Kieloch, A.2    Currie, R.A.3    Deak, M.4    Alessi, D.R.5
  • 63
    • 0033601217 scopus 로고    scopus 로고
    • Evidence that 3-phosphoinositide-dependent protein kinase-1 mediates phosphorylation of p70 S6 kinase in vivo at Thr-412 as well as Thr-252
    • Balendran, A, Currie, R., Armstrong, C. G., Avruch, J. & Alessi, D. R. Evidence that 3-phosphoinositide-dependent protein kinase-1 mediates phosphorylation of p70 S6 kinase in vivo at Thr-412 as well as Thr-252. J. Biol. Chem. 274, 37400-37406 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37400-37406
    • Balendran, A.1    Currie, R.2    Armstrong, C.G.3    Avruch, J.4    Alessi, D.R.5
  • 64
    • 0034609733 scopus 로고    scopus 로고
    • Identificatran of CISK, a new member of the SGK kinase family that promotes IL-3-dependent survival
    • Liu, D., Yang, X. & Songyang, Z. Identificatran of CISK, a new member of the SGK kinase family that promotes IL-3-dependent survival. Curr. Biol. 10, 1233-1236 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 1233-1236
    • Liu, D.1    Yang, X.2    Songyang, Z.3
  • 65
    • 0034743311 scopus 로고    scopus 로고
    • Ptdlns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40phox
    • Ellson, C. D. et al. Ptdlns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40phox. Nature Cell Biol. 3, 679-682 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 679-682
    • Ellson, C.D.1
  • 66
    • 0034946472 scopus 로고    scopus 로고
    • The PXdomains of p47phox and p40phox bind to lipid products of Pl(3)K
    • Kanal, F. et al. The PXdomains of p47phox and p40phox bind to lipid products of Pl(3)K. Nature Cell Biol. 3, 675-678 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 675-678
    • Kanal, F.1
  • 67
    • 0034947026 scopus 로고    scopus 로고
    • Phox domain interaction with Ptdlns(3)P targets the Vam7 t-SNARE to vacuole membranes
    • Cheever, M. L. et al. Phox domain interaction with Ptdlns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nature Cell Biol. 3, 613-618 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 613-618
    • Cheever, M.L.1
  • 68
    • 0035921426 scopus 로고    scopus 로고
    • Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides
    • Xu, J., Liu, D., Gill, G. & Songyang, Z. Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides. J. Cell. Biol. 20, 699-706 (2001).
    • (2001) J. Cell. Biol. , vol.20 , pp. 699-706
    • Xu, J.1    Liu, D.2    Gill, G.3    Songyang, Z.4
  • 69
    • 0028587370 scopus 로고
    • Identification of the TCL1 gene involved in T-cell malignancies
    • Virgilio, L. et al. Identification of the TCL1 gene involved in T-cell malignancies. Proc. Natl Acad. Sci. USA 91, 12530-12534 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12530-12534
    • Virgilio, L.1
  • 70
    • 0033636528 scopus 로고    scopus 로고
    • The protooncogene TCL1 is an Akt kinase coactivator
    • Laine, J., Kunstle, G., Obata, T., Sha, M. & Noguchi, M. The protooncogene TCL1 is an Akt kinase coactivator. Mol. Cell. 6, 395-407 (2000).
    • (2000) Mol. Cell. , vol.6 , pp. 395-407
    • Laine, J.1    Kunstle, G.2    Obata, T.3    Sha, M.4    Noguchi, M.5
  • 71
    • 0034911881 scopus 로고    scopus 로고
    • Synthesis and function of 3-phosphorylated inositol lipids
    • Vanhaesebroeck, B. et al. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70, 535-602 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 535-602
    • Vanhaesebroeck, B.1
  • 72
    • 0033811556 scopus 로고    scopus 로고
    • 5′ phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells
    • Taylor, V. et al. 5′ phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells. Mol. Cell. Biol. 20, 6860-6871 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6860-6871
    • Taylor, V.1
  • 73
    • 0033804532 scopus 로고    scopus 로고
    • Lipid phosphatases in the immune system. Semin
    • Krystal, G. Lipid phosphatases in the immune system. Semin. Immunol. 12, 397-403 (2000).
    • (2000) Immunol. , vol.12 , pp. 397-403
    • Krystal, G.1
  • 74
    • 0034681264 scopus 로고    scopus 로고
    • The multiple roles of PTEN in tumor suppression
    • D'Cristofano, A. & Pandolfi, P. P. The multiple roles of PTEN in tumor suppression. Cell 100, 387-390 (2000).
    • (2000) Cell , vol.100 , pp. 387-390
    • D'Cristofano, A.1    Pandolfi, P.P.2
  • 75
    • 0032590011 scopus 로고    scopus 로고
    • PlK3CA is implicated as an oncogene in ovarian cancer
    • Shayesteh, L. et al. PlK3CA is implicated as an oncogene in ovarian cancer. Nature Genet. 21, 99-102 (1999).
    • (1999) Nature Genet. , vol.21 , pp. 99-102
    • Shayesteh, L.1
  • 76
    • 0034742120 scopus 로고    scopus 로고
    • AKT1/PKB α kinase is frequently elevated in human cancers and its constitutive activation is required for oncogenic transformation in NIH3T3 cells
    • Sun, M. et al. AKT1/PKB α kinase is frequently elevated in human cancers and its constitutive activation is required for oncogenic transformation in NIH3T3 cells. Am. J. Pathol. 159, 431-437 (2001).
    • (2001) Am. J. Pathol. , vol.159 , pp. 431-437
    • Sun, M.1
  • 77
  • 78
    • 15444349266 scopus 로고    scopus 로고
    • Frequent inactivation of PTEN/MMAC1 in primary prostate cancer
    • Cairns, P. et al. Frequent inactivation of PTEN/MMAC1 in primary prostate cancer. Cancer Res. 57, 4997-5000 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 4997-5000
    • Cairns, P.1
  • 80
    • 0035220843 scopus 로고    scopus 로고
    • Mutational analysis of the PTEN gene in endometrial carcinoma and hyperplasia
    • Sun, H. et al. Mutational analysis of the PTEN gene in endometrial carcinoma and hyperplasia. Am. J. Clin. Pathol. 115, 32-38 (2001).
    • (2001) Am. J. Clin. Pathol. , vol.115 , pp. 32-38
    • Sun, H.1
  • 81
    • 0031004088 scopus 로고    scopus 로고
    • Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome
    • Liaw, D. et al. Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nature Genet. 16, 64-67 (1997).
    • (1997) Nature Genet. , vol.16 , pp. 64-67
    • Liaw, D.1
  • 82
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama, T. & Dixon, J. E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273, 13375-13378 (1998). The paper that turned the tide in understanding PTEN's role.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 83
    • 0032529189 scopus 로고    scopus 로고
    • Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor
    • Paradis, S. & Ruvkun, G. Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals from AGE-1 PI3 kinase to the DAF-16 transcription factor. Genes Dev. 12, 2488-2498 (1998). The first genetically identified PKB/AKT target, DAF-16, is a forkhead-like transcription factor - a prelude to the identification of mammalian homologues of PKB/AKT substrates.
    • (1998) Genes Dev. , vol.12 , pp. 2488-2498
    • Paradis, S.1    Ruvkun, G.2
  • 84
    • 0007588936 scopus 로고    scopus 로고
    • Drosophila phosphoinositide-dependent kinase-1 regulates apoptosis and growth via the phosphoinositide 3 kinase-dependent signaling pathway
    • Cho, K. S. et al. Drosophila phosphoinositide-dependent kinase-1 regulates apoptosis and growth via the phosphoinositide 3 kinase-dependent signaling pathway. Proc. Natl Acad. Sci. USA 98, 6144-6149 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6144-6149
    • Cho, K.S.1
  • 85
    • 0034613164 scopus 로고    scopus 로고
    • Regulation of C. elegans life-span by insulin like signaling in the nervous system
    • Wolkow, C. A., Kimura, K. D., Lee, M. S. & Ruvkun, G. Regulation of C. elegans life-span by insulin like signaling in the nervous system. Science 290, 147-150 (2000).
    • (2000) Science , vol.290 , pp. 147-150
    • Wolkow, C.A.1    Kimura, K.D.2    Lee, M.S.3    Ruvkun, G.4
  • 86
    • 0035868890 scopus 로고    scopus 로고
    • Regulation of DAF-2 receptor signaling by human insulin and ins-1, a member of the unusually large and diverse C. elegans insulin gene family
    • Pierce, S. B. et al. Regulation of DAF-2 receptor signaling by human insulin and ins-1, a member of the unusually large and diverse C. elegans insulin gene family. Genes Dev. 15, 672-686 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 672-686
    • Pierce, S.B.1
  • 87
    • 0033151613 scopus 로고    scopus 로고
    • A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans
    • Paradis, S., Ailion, M., Token A., Thomas, J. H. & Ruvkun, G. A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans. Genes Dev. 13, 1438-1452 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1438-1452
    • Paradis, S.1    Ailion, M.2    Token, A.3    Thomas, J.H.4    Ruvkun, G.5
  • 88
    • 0034680008 scopus 로고    scopus 로고
    • The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila
    • Scanga, S. E. et al.The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila. Oncogene 19, 3971-3977 (2000).
    • (2000) Oncogene , vol.19 , pp. 3971-3977
    • Scanga, S.E.1
  • 89
    • 0032493029 scopus 로고    scopus 로고
    • Genetic analysis of protein kinase B (AKT) in Drosophila
    • Staveley, B. E. et al. Genetic analysis of protein kinase B (AKT) in Drosophila. Curr. Biol. 8, 599-602 (1998). Genetic evidence of a conserved role for PKB/AKT in suppressing apoptosis.
    • (1998) Curr. Biol. , vol.8 , pp. 599-602
    • Staveley, B.E.1
  • 90
    • 0033258521 scopus 로고    scopus 로고
    • Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB
    • Verdu, J., Buratovich, M. A., Wilder, E. L. & Birnbaum, M. J. Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/PKB. Nature Cell Biol. 1, 500-506 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 500-506
    • Verdu, J.1    Buratovich, M.A.2    Wilder, E.L.3    Birnbaum, M.J.4
  • 91
    • 0029147402 scopus 로고
    • A phosphatidylinositol (Pl) kinase gene family in Dictyostelium discoideum: Biological roles of putative mammalian p110 and yeast Vps34p Pl3-kinase homologs during growth and development
    • Zhou, K., Takegawa, K., Emr, S. D. & Firtel, R. A. A phosphatidylinositol (Pl) kinase gene family in Dictyostelium discoideum: biological roles of putative mammalian p110 and yeast Vps34p Pl3-kinase homologs during growth and development. Mol. Cell. Biol. 15, 5645-5656 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5645-5656
    • Zhou, K.1    Takegawa, K.2    Emr, S.D.3    Firtel, R.A.4
  • 92
    • 0035881962 scopus 로고    scopus 로고
    • RasC is required for optimal activation of adenylyl cyclase and Akt/PKB during aggregation
    • Lim, C. J., Spiegelman, G. B. & Weeks, G. RasC is required for optimal activation of adenylyl cyclase and Akt/PKB during aggregation. EMBO J. 20, 4490-4499 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4490-4499
    • Lim, C.J.1    Spiegelman, G.B.2    Weeks, G.3
  • 93
    • 0033560747 scopus 로고    scopus 로고
    • Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium
    • Meili, R. et al. Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium. EMBO J. 18, 2092-2105 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2092-2105
    • Meili, R.1
  • 94
    • 0035947085 scopus 로고    scopus 로고
    • Control of cell polarity and chemotaxis by Akt/PKB and Pl3 kinase through the regulation of PAKa
    • Chung, C. Y., Potikyan, G. & Firtel, R. A. Control of cell polarity and chemotaxis by Akt/PKB and Pl3 kinase through the regulation of PAKa. Mol. Cell 7, 937-947 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 937-947
    • Chung, C.Y.1    Potikyan, G.2    Firtel, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.