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Volumn 17, Issue 2, 2005, Pages 150-157

Recent advances in the protein kinase B signaling pathway

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3; PHOSPHOINOSITIDE DEPENDENT KINASE 1; PHOSPHOTRANSFERASE; PROTEIN KINASE B; UNCLASSIFIED DRUG;

EID: 15044363028     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2005.02.010     Document Type: Review
Times cited : (321)

References (56)
  • 1
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • L.C. Cantley The phosphoinositide 3-kinase pathway Science 296 2002 1655 1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 2
    • 0142227019 scopus 로고    scopus 로고
    • Targeting the PI3K-Akt pathway in human cancer: Rationale and promise
    • J. Luo, B.D. Manning, and L.C. Cantley Targeting the PI3K-Akt pathway in human cancer: rationale and promise Cancer Cell 4 2003 257 262
    • (2003) Cancer Cell , vol.4 , pp. 257-262
    • Luo, J.1    Manning, B.D.2    Cantley, L.C.3
  • 3
    • 0142011466 scopus 로고    scopus 로고
    • PTEN: From pathology to biology
    • M.L. Sulis, and R. Parsons PTEN: from pathology to biology Trends Cell Biol 13 2003 478 483
    • (2003) Trends Cell Biol , vol.13 , pp. 478-483
    • Sulis, M.L.1    Parsons, R.2
  • 4
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • A. Bellacosa, J.R. Testa, S.P. Staal, and P.N. Tsichlis A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region Science 254 1991 274 277
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 5
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • I. Vivanco, and C.L. Sawyers The phosphatidylinositol 3-kinase AKT pathway in human cancer Nat Rev Cancer 2 2002 489 501
    • (2002) Nat Rev Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 6
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • D.A. Cross, D.R. Alessi, P. Cohen, M. Andjelkovich, and B.A. Hemmings Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B Nature 378 1995 785 789
    • (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
  • 7
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • B.W. Doble, and J.R. Woodgett GSK-3: tricks of the trade for a multi-tasking kinase J Cell Sci 116 2003 1175 1186
    • (2003) J Cell Sci , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 8
    • 0037862006 scopus 로고    scopus 로고
    • Unravelling the activation mechanisms of protein kinase B/Akt
    • M.P. Scheid, and J.R. Woodgett Unravelling the activation mechanisms of protein kinase B/Akt FEBS Lett 546 2003 108 112
    • (2003) FEBS Lett , vol.546 , pp. 108-112
    • Scheid, M.P.1    Woodgett, J.R.2
  • 9
    • 0035921426 scopus 로고    scopus 로고
    • Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides
    • J. Xu, D. Liu, G. Gill, and Z. Songyang Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides J Cell Biol 154 2001 699 705
    • (2001) J Cell Biol , vol.154 , pp. 699-705
    • Xu, J.1    Liu, D.2    Gill, G.3    Songyang, Z.4
  • 10
    • 0037086001 scopus 로고    scopus 로고
    • Living with lethal PIP3 levels: Viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB
    • H. Stocker, M. Andjelkovic, S. Oldham, M. Laffargue, M.P. Wymann, B.A. Hemmings, and E. Hafen Living with lethal PIP3 levels: viability of flies lacking PTEN restored by a PH domain mutation in Akt/PKB Science 295 2002 2088 2091
    • (2002) Science , vol.295 , pp. 2088-2091
    • Stocker, H.1    Andjelkovic, M.2    Oldham, S.3    Laffargue, M.4    Wymann, M.P.5    Hemmings, B.A.6    Hafen, E.7
  • 11
    • 0034617281 scopus 로고    scopus 로고
    • A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta) and PKC-related kinase 2 by PDK1
    • A. Balendran, R.M. Biondi, P.C. Cheung, A. Casamayor, M. Deak, and D.R. Alessi A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta) and PKC-related kinase 2 by PDK1 J Biol Chem 275 2000 20806 20813
    • (2000) J Biol Chem , vol.275 , pp. 20806-20813
    • Balendran, A.1    Biondi, R.M.2    Cheung, P.C.3    Casamayor, A.4    Deak, M.5    Alessi, D.R.6
  • 12
    • 0037107414 scopus 로고    scopus 로고
    • A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation
    • M. Frodin, T.L. Antal, B.A. Dummler, C.J. Jensen, M. Deak, S. Gammeltoft, and R.M. Biondi A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation EMBO J 21 2002 5396 5407
    • (2002) EMBO J , vol.21 , pp. 5396-5407
    • Frodin, M.1    Antal, T.L.2    Dummler, B.A.3    Jensen, C.J.4    Deak, M.5    Gammeltoft, S.6    Biondi, R.M.7
  • 13
    • 0035882103 scopus 로고    scopus 로고
    • The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
    • R.M. Biondi, A. Kieloch, R.A. Currie, M. Deak, and D.R. Alessi The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB EMBO J 20 2001 4380 4390
    • (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
  • 14
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • J. Yang, P. Cron, V. Thompson, V.M. Good, D. Hess, B.A. Hemmings, and D. Barford Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation Mol Cell 9 2002 1227 1240
    • (2002) Mol Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 15
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-P
    • J. Yang, P. Cron, V.M. Good, V. Thompson, B.A. Hemmings, and D. Barford Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-P Nat Struct Biol 9 2002 940 944
    • (2002) Nat Struct Biol , vol.9 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 17
    • 0034176579 scopus 로고    scopus 로고
    • The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells
    • M.R. Williams, J.S. Arthur, A. Balendran, J. van der Kaay, V. Poli, P. Cohen, and D.R. Alessi The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells Curr Biol 10 2000 439 448
    • (2000) Curr Biol , vol.10 , pp. 439-448
    • Williams, M.R.1    Arthur, J.S.2    Balendran, A.3    Van Der Kaay, J.4    Poli, V.5    Cohen, P.6    Alessi, D.R.7
  • 22
    • 0036333737 scopus 로고    scopus 로고
    • Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B
    • M.P. Scheid, P.A. Marignani, and J.R. Woodgett Multiple phosphoinositide 3-kinase-dependent steps in activation of protein kinase B Mol Cell Biol 22 2002 6247 6260
    • (2002) Mol Cell Biol , vol.22 , pp. 6247-6260
    • Scheid, M.P.1    Marignani, P.A.2    Woodgett, J.R.3
  • 23
    • 0042967831 scopus 로고    scopus 로고
    • In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation
    • B.J. Collins, M. Deak, J.S. Arthur, L.J. Armit, and D.R. Alessi In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation EMBO J 22 2003 4202 4211 This paper demonstrates, in an elegant manner, the importance of the PIF-pocket of PDK1 on phosphorylation of certain of its substrate proteins in embryonic stem cells.
    • (2003) EMBO J , vol.22 , pp. 4202-4211
    • Collins, B.J.1    Deak, M.2    Arthur, J.S.3    Armit, L.J.4    Alessi, D.R.5
  • 24
    • 0037107414 scopus 로고    scopus 로고
    • A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation
    • M. Frodin, T.L. Antal, B.A. Dummler, C.J. Jensen, M. Deak, S. Gammeltoft, and R.M. Biondi A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation EMBO J 21 2002 5396 5407
    • (2002) EMBO J , vol.21 , pp. 5396-5407
    • Frodin, M.1    Antal, T.L.2    Dummler, B.A.3    Jensen, C.J.4    Deak, M.5    Gammeltoft, S.6    Biondi, R.M.7
  • 25
    • 6444241901 scopus 로고    scopus 로고
    • Differential roles of PDK1- and PDK2-phosphorylation sites in the yeast AGC kinases Ypk1, Pkc1 and Sch9
    • F.M. Roelants, P.D. Torrance, and J. Thorner Differential roles of PDK1- and PDK2-phosphorylation sites in the yeast AGC kinases Ypk1, Pkc1 and Sch9 Microbiology 150 2004 3289 3304
    • (2004) Microbiology , vol.150 , pp. 3289-3304
    • Roelants, F.M.1    Torrance, P.D.2    Thorner, J.3
  • 27
    • 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
    • M.M. Hill, M. Andjelkovic, D.P. Brazil, S. Ferrari, D. Fabbro, and B.A. Hemmings 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 2001 25643 25646
    • (2001) J Biol Chem , vol.276 , pp. 25643-25646
    • Hill, M.M.1    Andjelkovic, M.2    Brazil, D.P.3    Ferrari, S.4    Fabbro, D.5    Hemmings, B.A.6
  • 28
    • 0038724824 scopus 로고    scopus 로고
    • The role of integrin-linked kinase (ILK) in cancer progression
    • S. Persad, and S. Dedhar The role of integrin-linked kinase (ILK) in cancer progression Cancer Metastasis Rev 22 2003 375 384
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 375-384
    • Persad, S.1    Dedhar, S.2
  • 29
    • 0037109063 scopus 로고    scopus 로고
    • Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase
    • J.T. Deng, C. Sutherland, D.L. Brautigan, M. Eto, and M.P. Walsh Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase Biochem J 367 2002 517 524
    • (2002) Biochem J , vol.367 , pp. 517-524
    • Deng, J.T.1    Sutherland, C.2    Brautigan, D.L.3    Eto, M.4    Walsh, M.P.5
  • 30
    • 0037666792 scopus 로고    scopus 로고
    • Conditional knock-out of integrin-linked kinase demonstrates an essential role in protein kinase B/Akt activation
    • A.A. Troussard, N.M. Mawji, C. Ong, A. Mui, R. St-Arnaud, and S. Dedhar Conditional knock-out of integrin-linked kinase demonstrates an essential role in protein kinase B/Akt activation J Biol Chem 278 2003 22374 22378 This study provides genetic evidence for a role of ILK kinase activity in the phosphorylation of PKB at Ser473, using conditional knockout and siRNA approaches.
    • (2003) J Biol Chem , vol.278 , pp. 22374-22378
    • Troussard, A.A.1    Mawji, N.M.2    Ong, C.3    Mui, A.4    St-Arnaud, R.5    Dedhar, S.6
  • 31
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • C.G. Zervas, S.L. Gregory, and N.H. Brown Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane J Cell Biol 152 2001 1007 1018
    • (2001) J Cell Biol , vol.152 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3
  • 32
    • 0037162291 scopus 로고    scopus 로고
    • Identification of a plasma membrane Raft-associated PKB Ser473 kinase activity that is distinct from ILK and PDK1
    • M.M. Hill, J. Feng, and B.A. Hemmings Identification of a plasma membrane Raft-associated PKB Ser473 kinase activity that is distinct from ILK and PDK1 Curr Biol 12 2002 1251 1255
    • (2002) Curr Biol , vol.12 , pp. 1251-1255
    • Hill, M.M.1    Feng, J.2    Hemmings, B.A.3
  • 34
    • 0037821794 scopus 로고    scopus 로고
    • Phosphoinositide-dependent kinase-2 is a distinct protein kinase enriched in a novel cytoskeletal fraction associated with adipocyte plasma membranes
    • R.C. Hresko, H. Murata, and M. Mueckler Phosphoinositide-dependent kinase-2 is a distinct protein kinase enriched in a novel cytoskeletal fraction associated with adipocyte plasma membranes J Biol Chem 278 2003 21615 21622
    • (2003) J Biol Chem , vol.278 , pp. 21615-21622
    • Hresko, R.C.1    Murata, H.2    Mueckler, M.3
  • 35
    • 0037072272 scopus 로고    scopus 로고
    • Characterization of PDK2 activity against protein kinase Bγ
    • C.P. Hodgkinson, E.M. Sale, and G.J. Sale Characterization of PDK2 activity against protein kinase Bγ Biochemistry 41 2002 10351 10359
    • (2002) Biochemistry , vol.41 , pp. 10351-10359
    • Hodgkinson, C.P.1    Sale, E.M.2    Sale, G.J.3
  • 36
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • J. Feng, J. Park, P. Cron, D. Hess, and B.A. Hemmings Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase J Biol Chem 279 2004 41189 41196 One of several important papers characterizing putative PDK2 activities.
    • (2004) J Biol Chem , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 37
    • 0032167446 scopus 로고    scopus 로고
    • A targeted DNA-PKcs-null mutation reveals DNA-PK-independent functions for KU in V(D)J recombination
    • Y. Gao, J. Chaudhuri, C. Zhu, L. Davidson, D.T. Weaver, and F.W. Alt A targeted DNA-PKcs-null mutation reveals DNA-PK-independent functions for KU in V(D)J recombination Immunity 9 1998 367 376
    • (1998) Immunity , vol.9 , pp. 367-376
    • Gao, Y.1    Chaudhuri, J.2    Zhu, C.3    Davidson, L.4    Weaver, D.T.5    Alt, F.W.6
  • 40
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • E. Jacinto, R. Loewith, A. Schmidt, S. Lin, M.A. Ruegg, A. Hall, and M.N. Hall Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive Nat Cell Biol 6 2004 1122 1128 This paper demonstrates the existence of a second mTOR complex in mammalian cells that is not inhibited by rapamycin, which raises the possibility of roles for mTOR in rapamycin-insensitive processes.
    • (2004) Nat Cell Biol , vol.6 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3    Lin, S.4    Ruegg, M.A.5    Hall, A.6    Hall, M.N.7
  • 41
    • 0344270855 scopus 로고    scopus 로고
    • Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): A potential regulatory mechanism for PDK-1 function
    • M.A. Lim, C.K. Kikani, M.J. Wick, and L.Q. Dong Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): a potential regulatory mechanism for PDK-1 function Proc Natl Acad Sci USA 100 2003 14006 14011 This paper demonstrated that nuclear transport of PDK-1 has the potential to be regulated rather than being a passive process and identified a functional nuclear export sequence (NES) in the molecule.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14006-14011
    • Lim, M.A.1    Kikani, C.K.2    Wick, M.J.3    Dong, L.Q.4
  • 42
    • 14844357714 scopus 로고    scopus 로고
    • Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation
    • in press.
    • Scheid MP, Parsons M, Woodgett JR: Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation. Mol Cell Biol 2005, in press. This paper identifies PI3K-dependent phosphorylation of PDK-1 to be a means to regulate its nuclear entry and exit, providing another layer of the regulation to this protein kinase.
    • (2005) Mol Cell Biol
    • Scheid, M.P.1    Parsons, M.2    Woodgett, J.R.3
  • 43
    • 2342565881 scopus 로고    scopus 로고
    • Advances in protein kinase B signalling: AKTion on multiple fronts
    • D.P. Brazil, Z.Z. Yang, and B.A. Hemmings Advances in protein kinase B signalling: AKTion on multiple fronts Trends Biochem Sci 29 2004 233 242
    • (2004) Trends Biochem Sci , vol.29 , pp. 233-242
    • Brazil, D.P.1    Yang, Z.Z.2    Hemmings, B.A.3
  • 44
    • 0035913188 scopus 로고    scopus 로고
    • Oncogenic transformation induced by membrane-targeted Akt2 and Akt3
    • I. Mende, S. Malstrom, P.N. Tsichlis, P.K. Vogt, and M. Aoki Oncogenic transformation induced by membrane-targeted Akt2 and Akt3 Oncogene 20 2001 4419 4423
    • (2001) Oncogene , vol.20 , pp. 4419-4423
    • Mende, I.1    Malstrom, S.2    Tsichlis, P.N.3    Vogt, P.K.4    Aoki, M.5
  • 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
    • J. Hutchinson, J. Jin, R.D. Cardiff, J.R. Woodgett, and W.J. Muller Activation of Akt (protein kinase B) in mammary epithelium provides a critical cell survival signal required for tumor progression Mol Cell Biol 21 2001 2203 2212
    • (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
    • 2342527930 scopus 로고    scopus 로고
    • Activation of Akt-1 (PKB-α) can accelerate ErbB-2-mediated mammary tumorigenesis but suppresses tumor invasion
    • J.N. Hutchinson, J. Jin, R.D. Cardiff, J.R. Woodgett, and W.J. Muller Activation of Akt-1 (PKB-α) can accelerate ErbB-2-mediated mammary tumorigenesis but suppresses tumor invasion Cancer Res 64 2004 3171 3178
    • (2004) Cancer Res , vol.64 , pp. 3171-3178
    • Hutchinson, J.N.1    Jin, J.2    Cardiff, R.D.3    Woodgett, J.R.4    Muller, W.J.5
  • 48
    • 0242361561 scopus 로고    scopus 로고
    • Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes
    • V.K. Rajasekhar, A. Viale, N.D. Socci, M. Wiedmann, X. Hu, and E.C. Holland Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes Mol Cell 12 2003 889 901
    • (2003) Mol Cell , vol.12 , pp. 889-901
    • Rajasekhar, V.K.1    Viale, A.2    Socci, N.D.3    Wiedmann, M.4    Hu, X.5    Holland, E.C.6
  • 49
    • 0037229714 scopus 로고    scopus 로고
    • Overexpression of AKT2/protein kinase Bβ leads to up-regulation of β1 integrins, increased invasion, and metastasis of human breast and ovarian cancer cells
    • M.J. Arboleda, J.F. Lyons, F.F. Kabbinavar, M.R. Bray, B.E. Snow, R. Ayala, M. Danino, B.Y. Karlan, and D.J. Slamon Overexpression of AKT2/protein kinase Bβ leads to up-regulation of β1 integrins, increased invasion, and metastasis of human breast and ovarian cancer cells Cancer Res 63 2003 196 206 This study provides insight into the biological consequences of increased levels of the β isoform of PKB on tumor cell properties.
    • (2003) Cancer Res , vol.63 , pp. 196-206
    • Arboleda, M.J.1    Lyons, J.F.2    Kabbinavar, F.F.3    Bray, M.R.4    Snow, B.E.5    Ayala, R.6    Danino, M.7    Karlan, B.Y.8    Slamon, D.J.9
  • 50
    • 19944433628 scopus 로고    scopus 로고
    • Identification and characterization of pleckstrin homology domain dependent and isozyme specific Akt inhibitors
    • S.F. Barnett, D. Defeo-Jones, S. Fu, P.J. Hancock, K.M. Haskell, R.E. Jones, J.A. Kahana, A.M. Kral, K. Leander, and L.L. Lee Identification and characterization of pleckstrin homology domain dependent and isozyme specific Akt inhibitors Biochem J 385 2005 399 408 This paper from Merck introduces isoform-selective PKB inhibitors that act through binding to both the PH and protein kinase domains. These reagents should prove very useful in understanding PKB functions.
    • (2005) Biochem J , vol.385 , pp. 399-408
    • Barnett, S.F.1    Defeo-Jones, D.2    Fu, S.3    Hancock, P.J.4    Haskell, K.M.5    Jones, R.E.6    Kahana, J.A.7    Kral, A.M.8    Leander, K.9    Lee, L.L.10
  • 51
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 β: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • R. Dajani, E. Fraser, S.M. Roe, N. Young, V. Good, T.C. Dale, and L.H. Pearl Crystal structure of glycogen synthase kinase 3 β: structural basis for phosphate-primed substrate specificity and autoinhibition Cell 105 2001 721 732
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 53
    • 0034969088 scopus 로고    scopus 로고
    • A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation
    • S. Frame, P. Cohen, and R.M. Biondi A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation Mol Cell 7 2001 1321 1327
    • (2001) Mol Cell , vol.7 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 54
    • 1642494586 scopus 로고    scopus 로고
    • Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event
    • A. Cole, S. Frame, and P. Cohen Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event Biochem J 377 2004 249 255
    • (2004) Biochem J , vol.377 , pp. 249-255
    • Cole, A.1    Frame, S.2    Cohen, P.3
  • 55
    • 12944250922 scopus 로고    scopus 로고
    • Phosphorylation and inactivation of glycogen synthase kinase-3 by both protein kinase a and protein kinase B
    • X. Fang, Y. Lu, S.X. Yu, Y. Lu, R.C. Bast, J.R. Woodgett, and G.B. Mills Phosphorylation and inactivation of glycogen synthase kinase-3 by both protein kinase A and protein kinase B Proc Natl Acad Sci USA 97 2000 11960 11965
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11960-11965
    • Fang, X.1    Lu, Y.2    Yu, S.X.3    Lu, Y.4    Bast, R.C.5    Woodgett, J.R.6    Mills, G.B.7
  • 56
    • 0036120653 scopus 로고    scopus 로고
    • Convergence of multiple signaling cascades at glycogen synthase kinase 3: Edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase C-dependent intracellular pathway
    • X. Fang, S. Yu, J.L. Tanyi, Y. Lu, J.R. Woodgett, and G.B. Mills Convergence of multiple signaling cascades at glycogen synthase kinase 3: Edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase C-dependent intracellular pathway Mol Cell Biol 22 2002 2099 2110
    • (2002) Mol Cell Biol , vol.22 , pp. 2099-2110
    • Fang, X.1    Yu, S.2    Tanyi, J.L.3    Lu, Y.4    Woodgett, J.R.5    Mills, G.B.6


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