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Volumn 108, Issue 46, 2011, Pages

Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity

Author keywords

Inhibitors hijacking kinase activation; Kinase priming phosphorylations; PP2A; Protein kinase B

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; AKT 1 PROTEIN; GLYCOGEN SYNTHASE KINASE 3; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN KINASE B; PROTEIN KINASE B BETA; UNCLASSIFIED DRUG;

EID: 81755163634     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1109879108     Document Type: Article
Times cited : (67)

References (42)
  • 1
    • 0032881288 scopus 로고    scopus 로고
    • AKT/PKB and other D3 phosphoinositide-regulated kinases: Kinase acvtivation by phosphoinositide-dependent phosphorylation
    • Chan TO, Rittenhouse SE, Tsichlis PN (1999) AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase acvtivation by phosphoinositide- dependent phosphorylation. Ann Rev Biochem 68:965-1015.
    • (1999) Ann Rev Biochem , vol.68 , pp. 965-1015
    • Chan, T.O.1    Rittenhouse, S.E.2    Tsichlis, P.N.3
  • 3
    • 34247116441 scopus 로고    scopus 로고
    • Physiological roles of PKB/Akt isoforms in development and disease
    • DOI 10.1042/BST0350231
    • Dummler B, Hemmings BA (2007) Physiological roles of PKB/Akt isoforms in development and disease. Biochem Soc Trans 35:231-235. (Pubitemid 46596476)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.2 , pp. 231-235
    • Dummler, B.1    Hemmings, B.A.2
  • 6
    • 0036154215 scopus 로고    scopus 로고
    • Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes
    • DOI 10.1016/S0898-6568(01)00238-8, PII S0898656801002388
    • Resjo S, et al. (2002) Protein phosphatase 2 A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes. Cell Signal 14:231-238. (Pubitemid 34102452)
    • (2002) Cellular Signalling , vol.14 , Issue.3 , pp. 231-238
    • Resjo, S.1    Goransson, O.2    Harndahl, L.3    Zolnierowicz, S.4    Manganiello, V.5    Degerman, E.6
  • 7
    • 38349190654 scopus 로고    scopus 로고
    • Regulation of phosphorylation of Thr-308 of Akt, cell proliferation, and survival by the B55alpha regulatory subunit targeting of the protein phosphatase 2 A holoenzyme to Akt
    • Kuo YC, et al. (2008) Regulation of phosphorylation of Thr-308 of Akt, cell proliferation, and survival by the B55alpha regulatory subunit targeting of the protein phosphatase 2 A holoenzyme to Akt. J Biol Chem 283:1882-1892.
    • (2008) J Biol Chem , vol.283 , pp. 1882-1892
    • Kuo, Y.C.1
  • 8
    • 56349087537 scopus 로고    scopus 로고
    • The protein phosphatase PP2A-B′ subunit Widerborst is a negative regulator of cytoplasmic activated Akt and lipid metabolism in Drosophila
    • Vereshchagina N, Ramel MC, Bitoun E, Wilson C (2008) The protein phosphatase PP2A-B′ subunit Widerborst is a negative regulator of cytoplasmic activated Akt and lipid metabolism in Drosophila. J Cell Sci 121:3383-3392.
    • (2008) J Cell Sci , vol.121 , pp. 3383-3392
    • Vereshchagina, N.1    Ramel, M.C.2    Bitoun, E.3    Wilson, C.4
  • 9
    • 61349123235 scopus 로고    scopus 로고
    • A PP2A regulatory subunit regulates C. elegans insulin/ IGF-1 signaling by modulating AKT-1 phosphorylation
    • Padmanabhan S, et al. (2009) A PP2A regulatory subunit regulates C. elegans insulin/ IGF-1 signaling by modulating AKT-1 phosphorylation. Cell 136:939-951.
    • (2009) Cell , vol.136 , pp. 939-951
    • Padmanabhan, S.1
  • 10
  • 13
    • 58849120491 scopus 로고    scopus 로고
    • Role of a novel PH-kinase domain interface in PKB/Akt regulation: Structural mechanism for allosteric inhibition
    • Calleja V, Laguerre M, Parker PJ, Larijani B (2009) Role of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibition. PLoS Biol 7:e17.
    • (2009) PLoS Biol , vol.7
    • Calleja, V.1    Laguerre, M.2    Parker, P.J.3    Larijani, B.4
  • 14
    • 77958576132 scopus 로고    scopus 로고
    • Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition
    • Wu WI, et al. (2010) Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition. PLoS One 5:e12913.
    • (2010) PLoS One , vol.5
    • Wu, W.I.1
  • 16
    • 61849181403 scopus 로고    scopus 로고
    • AKT inhibitor, GSK690693, induces growth inhibition and apoptosis in acute lymphoblastic leukemia cell lines
    • Levy DS, Kahana JA, Kumar R (2009) AKT inhibitor, GSK690693, induces growth inhibition and apoptosis in acute lymphoblastic leukemia cell lines. Blood 113:1723-1729.
    • (2009) Blood , vol.113 , pp. 1723-1729
    • Levy, D.S.1    Kahana, J.A.2    Kumar, R.3
  • 17
    • 67650337799 scopus 로고    scopus 로고
    • Inhibitor hijacking of Akt activation
    • Okuzumi T, et al. (2009) Inhibitor hijacking of Akt activation. Nat Chem Biol 5:484-493.
    • (2009) Nat Chem Biol , vol.5 , pp. 484-493
    • Okuzumi, T.1
  • 19
  • 20
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • DOI 10.1016/S0092-8674(02)00741-9
    • Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:275-282. (Pubitemid 34606870)
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 21
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • DOI 10.1016/S1097-2765(02)00550-6
    • Yang J, et al. (2002) Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol Cell 9:1227-1240. (Pubitemid 34722302)
    • (2002) Molecular Cell , vol.9 , Issue.6 , 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
  • 25
    • 33846781365 scopus 로고    scopus 로고
    • Targeted inhibition of the extracellular signal-regulated kinase kinase pathway with AZD6244 (ARRY-142886) in the treatment of hepatocellular carcinoma
    • DOI 10.1158/1535-7163.MCT-06-0436
    • Huynh H, Soo KC, Chow PK, Tran E (2007) Targeted inhibition of the extracellular signal-regulated kinase kinase pathway with AZD6244 (ARRY-142886) in the treatment of hepatocellular carcinoma. Mol Cancer Ther 6:138-146. (Pubitemid 46206676)
    • (2007) Molecular Cancer Therapeutics , vol.6 , Issue.1 , pp. 138-146
    • Huynh, H.1    Soo, K.C.2    Chow, P.K.H.3    Tran, E.4
  • 26
    • 66749155533 scopus 로고    scopus 로고
    • Resistance to mitogen-activated protein kinase kinase (MEK) inhibitors correlates with up-regulation of the MEK/extracellular signal-regulated kinase pathway in hepatocellular carcinoma cells
    • Yip-Schneider MT, et al. (2009) Resistance to mitogen-activated protein kinase kinase (MEK) inhibitors correlates with up-regulation of the MEK/extracellular signal-regulated kinase pathway in hepatocellular carcinoma cells. J Pharmacol Exp Ther 329:1063-1070.
    • (2009) J Pharmacol Exp Ther , vol.329 , pp. 1063-1070
    • Yip-Schneider, M.T.1
  • 27
    • 15744380263 scopus 로고    scopus 로고
    • Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition
    • Ohren JF, et al. (2004) Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat Struct Mol Biol 11:1192-1197.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1192-1197
    • Ohren, J.F.1
  • 28
    • 67349125149 scopus 로고    scopus 로고
    • PKC maturation is promoted by nucleotide pocket occupation independently of intrinsic kinase activity
    • Cameron AJ, Escribano C, Saurin AT, Kostelecky B, Parker PJ (2009) PKC maturation is promoted by nucleotide pocket occupation independently of intrinsic kinase activity. Nat Struct Mol Biol 16:624-630.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 624-630
    • Cameron, A.J.1    Escribano, C.2    Saurin, A.T.3    Kostelecky, B.4    Parker, P.J.5
  • 29
    • 0037051553 scopus 로고    scopus 로고
    • Dephosphorylation of PKCdelta by protein phosphatase 2Ac and its inhibition by nucleotides
    • DOI 10.1016/S0014-5793(02)02500-0, PII S0014579302025000
    • Srivastava J, Goris J, Dilworth SM, Parker PJ (2002) Dephosphorylation of PKCdelta by protein phosphatase 2Ac and its inhibition by nucleotides. FEBS Lett 516:265-269. (Pubitemid 34311973)
    • (2002) FEBS Letters , vol.516 , Issue.1-3 , pp. 265-269
    • Srivastava, J.1    Goris, J.2    Dilworth, S.M.3    Parker, P.J.4
  • 30
    • 0032439795 scopus 로고    scopus 로고
    • Purine nucleotide- and sugar phosphate-induced inhibition of the carboxyl methylation and catalysis of protein phosphatase-2A in insulin-secreting cells: Protection by divalent cations
    • DOI 10.1023/A:1020148729747
    • Kowluru A, Metz SA (1998) Purine nucleotide- and sugar phosphate-induced inhibition of the carboxyl methylation and catalysis of protein phosphatase-2A in insulin-secreting cells: protection by divalent cations. Biosci Rep 18:171-186. (Pubitemid 29026676)
    • (1998) Bioscience Reports , vol.18 , Issue.4 , pp. 171-186
    • Kowluru, A.1    Metz, S.A.2
  • 31
    • 0032557646 scopus 로고    scopus 로고
    • Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB
    • van Weeren PC, de Bruyn KM, de Vries-Smits AM, van Lint J, Burgering BM (1998) Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB. J Biol Chem 273:13150-13156.
    • (1998) J Biol Chem , vol.273 , pp. 13150-13156
    • Van Weeren, P.C.1    De Bruyn, K.M.2    De Vries-Smits, A.M.3    Van Lint, J.4    Burgering, B.M.5
  • 33
    • 79955844083 scopus 로고    scopus 로고
    • Briefly bound to activate: Transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis
    • Bao ZQ, Jacobsen DM, Young MA (2011) Briefly bound to activate: transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis. Structure 19:675-690.
    • (2011) Structure , vol.19 , pp. 675-690
    • Bao, Z.Q.1    Jacobsen, D.M.2    Young, M.A.3
  • 35
    • 46249120772 scopus 로고    scopus 로고
    • Effect of metal ions on high-affinity binding of pseudosubstrate inhibitors to PKA
    • DOI 10.1042/BJ20071665
    • Zimmermann B, Schweinsberg S, Drewianka S, Herberg FW(2008) Effect of metal ions on high-affinity binding of pseudosubstrate inhibitors to PKA. Biochem J 413:93-101. (Pubitemid 351946865)
    • (2008) Biochemical Journal , vol.413 , Issue.1 , pp. 93-101
    • Zimmermann, B.1    Schweinsberg, S.2    Drewianka, S.3    Herberg, F.W.4
  • 36
    • 0027504662 scopus 로고
    • The phosphotyrosine phosphatase inhibitor vanadyl hydroperoxide induces morphological alterations, cytoskeletal rearrangements and increased adhesiveness in rat neutrophil leucocytes
    • Bennett PA, Dixon RJ, Kellie S (1993) The phosphotyrosine phosphatase inhibitor vanadyl hydroperoxide induces morphological alterations, cytoskeletal rearrangements and increased adhesiveness in rat neutrophil leucocytes. J Cell Sci 106:891-901. (Pubitemid 23346801)
    • (1993) Journal of Cell Science , vol.106 , Issue.3 , pp. 891-901
    • Bennett, P.A.1    Dixon, R.J.2    Kellie, S.3
  • 37
    • 0036605838 scopus 로고    scopus 로고
    • The synthetic peptide RPRAATF allows specific assay of akt activity in cell lysates
    • DOI 10.1006/abio.2002.5659
    • Bozinovski S, Cristiano BE, Marmy-Conus N, Pearson RB (2002) The synthetic peptide RPRAATF allows specific assay of Akt activity in cell lysates. Anal Biochem 305:32-39. (Pubitemid 34575822)
    • (2002) Analytical Biochemistry , vol.305 , Issue.1 , pp. 32-39
    • Bozinovski, S.1    Cristiano, B.E.2    Marmy-Conus, N.3    Pearson, R.B.4
  • 39
    • 0037034928 scopus 로고    scopus 로고
    • Interference with PDK1-Akt survival signaling pathway by UCN-01 (7-hydroxystaurosporine)
    • DOI 10.1038/sj/onc/1205225
    • Sato S, Fujita N, Tsuruo T (2002) Interference with PDK1-Akt survival signaling pathway by UCN-01 (7-hydroxystaurosporine). Oncogene 21:1727-1738. (Pubitemid 34259036)
    • (2002) Oncogene , vol.21 , Issue.11 , pp. 1727-1738
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 41
    • 67651142624 scopus 로고    scopus 로고
    • 2A-adenosine receptor in FVB Mice transiently increases contractile performance and rescues the heart failure phenotype in mice overexpressing the A1-adenosine receptor
    • 2A-adenosine receptor in FVB Mice transiently increases contractile performance and rescues the heart failure phenotype in mice overexpressing the A1-adenosine receptor. Clinical and Translational Science 1:126-133.
    • (2008) Clinical and Translational Science , vol.1 , pp. 126-133
    • Chan, T.O.H.F.1
  • 42
    • 67650500988 scopus 로고    scopus 로고
    • CHARMM: The biomolecular simulation program
    • Brooks BR, et al. (2009) CHARMM: the biomolecular simulation program. J Comput Chem 30:1545-1614.
    • (2009) J Comput Chem , vol.30 , pp. 1545-1614
    • Brooks, B.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.