메뉴 건너뛰기




Volumn 9, Issue 3, 2010, Pages 486-497

Regulation of Akt signaling activation by ubiquitination

Author keywords

Akt; E3 ligase; Kinase; mTORC2; NF B; PDK1; Phosphorylation; TRAF6; Tumorigenesis; Ubiquitination

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN KINASE B; SYNAPTOPHYSIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6;

EID: 77951917753     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.9.3.10508     Document Type: Review
Times cited : (121)

References (114)
  • 1
    • 0026095665 scopus 로고
    • A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region
    • Bellacosa A, Testa JR, Staal SP, Tsichlis PN. A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region. Science 1991; 254:274-7.
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 2
    • 0026006501 scopus 로고
    • Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families
    • Coffer PJ, Woodgett JR. Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families. Eur J Biochem 1991; 201:475-81.
    • (1991) Eur J Biochem , vol.201 , pp. 475-481
    • Coffer, P.J.1    Woodgett, J.R.2
  • 5
    • 68249093818 scopus 로고    scopus 로고
    • Targeting the phosphoinositide 3-kinase pathway in cancer
    • Liu P, Cheng H, Roberts TM, Zhao JJ. Targeting the phosphoinositide 3-kinase pathway in cancer. Nat Rev Drug Discov 2009; 8:627-44.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 627-644
    • Liu, P.1    Cheng, H.2    Roberts, T.M.3    Zhao, J.J.4
  • 6
    • 69549116880 scopus 로고    scopus 로고
    • The E3 ligase TRAF6 regulates Akt ubiquitination and activation
    • Yang WL, Wang J, Chan CH, Lee SW, Campos AD, Lamothe B, et al. The E3 ligase TRAF6 regulates Akt ubiquitination and activation. Science 2009; 325:1134-8.
    • (2009) Science , vol.325 , pp. 1134-1138
    • Yang, W.L.1    Wang, J.2    Chan, C.H.3    Lee, S.W.4    Campos, A.D.5    Lamothe, B.6
  • 7
    • 63649116570 scopus 로고    scopus 로고
    • Ubiquitylation in innate and adaptive immunity
    • Bhoj VG, Chen ZJ. Ubiquitylation in innate and adaptive immunity. Nature 2009; 458:430-7.
    • (2009) Nature , vol.458 , pp. 430-437
    • Bhoj, V.G.1    Chen, Z.J.2
  • 8
    • 0038784529 scopus 로고    scopus 로고
    • Are ubiquitination pathways central to Parkinson's disease?
    • Giasson BI, Lee VM. Are ubiquitination pathways central to Parkinson's disease? Cell 2003; 114:1-8.
    • (2003) Cell , vol.114 , pp. 1-8
    • Giasson, B.I.1    Lee, V.M.2
  • 9
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller D, Dikic I. Targeting the ubiquitin system in cancer therapy. Nature 2009; 458:438-44.
    • (2009) Nature , vol.458 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 10
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001; 70:503-33.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 11
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen ZJ, Sun LJ. Nonproteolytic functions of ubiquitin in cell signaling. Mol Cell 2009; 33:275-86.
    • (2009) Mol Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 12
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg C, Stenmark H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 2009; 458:445-52.
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 13
    • 64549154396 scopus 로고    scopus 로고
    • Diversity of polyubiquitin chains
    • Adhikari A, Chen ZJ. Diversity of polyubiquitin chains. Dev Cell 2009; 16:485-6.
    • (2009) Dev Cell , vol.16 , pp. 485-486
    • Adhikari, A.1    Chen, Z.J.2
  • 14
    • 27544473311 scopus 로고    scopus 로고
    • The ubiquitin ligase HectH9 regulates transcriptional activation by Myc and is essential for tumor cell proliferation
    • Adhikary S, Marinoni F, Hock A, Hulleman E, Popov N, Beier R, et al. The ubiquitin ligase HectH9 regulates transcriptional activation by Myc and is essential for tumor cell proliferation. Cell 2005; 123:409-21.
    • (2005) Cell , vol.123 , pp. 409-421
    • Adhikary, S.1    Marinoni, F.2    Hock, A.3    Hulleman, E.4    Popov, N.5    Beier, R.6
  • 16
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen MS, Grant R, Manke I, Minn K, Yu X, Yaffe MB, et al. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 2007; 131:901-14.
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1    Grant, R.2    Manke, I.3    Minn, K.4    Yu, X.5    Yaffe, M.B.6
  • 17
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • Sun SC. Deubiquitylation and regulation of the immune response. Nat Rev Immunol 2008; 8:501-11.
    • (2008) Nat Rev Immunol , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 18
    • 43049128529 scopus 로고    scopus 로고
    • Tenets of PTEN tumor suppression
    • Salmena L, Carracedo A, Pandolfi PP. Tenets of PTEN tumor suppression. Cell 2008; 133:403-14.
    • (2008) Cell , vol.133 , pp. 403-414
    • Salmena, L.1    Carracedo, A.2    Pandolfi, P.P.3
  • 20
  • 21
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NFkappaB pathway
    • Chen ZJ. Ubiquitin signalling in the NFkappaB pathway. Nat Cell Biol 2005; 7:758-65.
    • (2005) Nat Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 22
    • 79959378155 scopus 로고    scopus 로고
    • CYLD: A tumor suppressor deubiquitinase regulating NFkappaB activation and diverse biological processes
    • Sun SC. CYLD: a tumor suppressor deubiquitinase regulating NFkappaB activation and diverse biological processes. Cell Death Differ 2009.
    • (2009) Cell Death Differ
    • Sun, S.C.1
  • 23
    • 66649127621 scopus 로고    scopus 로고
    • Mutations of multiple genes cause deregulation of NFkappaB in diffuse large B-cell lymphoma
    • Compagno M, Lim WK, Grunn A, Nandula SV, Brahmachary M, Shen Q, et al. Mutations of multiple genes cause deregulation of NFkappaB in diffuse large B-cell lymphoma. Nature 2009; 459:717-21.
    • (2009) Nature , vol.459 , pp. 717-721
    • Compagno, M.1    Lim, W.K.2    Grunn, A.3    Nandula, S.V.4    Brahmachary, M.5    Shen, Q.6
  • 25
    • 66549086135 scopus 로고    scopus 로고
    • The NF-{kappa}B negative regulator TNFAIP3 (A20) is inactivated by somatic mutations and genomic deletions in marginal zone lymphomas
    • Novak U, Rinaldi A, Kwee I, Nandula SV, Rancoita PM, Compagno M, et al. The NF-{kappa}B negative regulator TNFAIP3 (A20) is inactivated by somatic mutations and genomic deletions in marginal zone lymphomas. Blood 2009; 113:4918-21.
    • (2009) Blood , vol.113 , pp. 4918-4921
    • Novak, U.1    Rinaldi, A.2    Kwee, I.3    Nandula, S.V.4    Rancoita, P.M.5    Compagno, M.6
  • 26
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins
    • DOI 10.1016/j.cell.2007.09.040, PII S0092867407012718
    • Mailand N, Bekker-Jensen S, Faustrup H, Melander F, Bartek J, Lukas C, et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 2007; 131:887-900. (Pubitemid 350138084)
    • (2007) Cell , vol.131 , Issue.5 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3    Melander, F.4    Bartek, J.5    Lukas, C.6    Lukas, J.7
  • 27
    • 36749025467 scopus 로고    scopus 로고
    • Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/ Brcc36 complex in response to DNA damage
    • Wang B, Elledge SJ. Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/ Brcc36 complex in response to DNA damage. Proc Natl Acad Sci USA 2007; 104:20759-63.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.J.2
  • 28
    • 48649110734 scopus 로고    scopus 로고
    • Identification of c-Cbl as a new ligase for insulinlike growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis
    • Sehat B, Andersson S, Girnita L, Larsson O. Identification of c-Cbl as a new ligase for insulinlike growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis. Cancer Res 2008; 68:5669-77.
    • (2008) Cancer Res , vol.68 , pp. 5669-5677
    • Sehat, B.1    Andersson, S.2    Girnita, L.3    Larsson, O.4
  • 29
    • 50249171794 scopus 로고    scopus 로고
    • Polyubiquitination of prolactin receptor stimulates its internalization, postinternalization sorting and degradation via the lysosomal pathway
    • Varghese B, Barriere H, Carbone CJ, Banerjee A, Swaminathan G, Plotnikov A, et al. Polyubiquitination of prolactin receptor stimulates its internalization, postinternalization sorting and degradation via the lysosomal pathway. Mol Cell Biol 2008; 28:5275-87.
    • (2008) Mol Cell Biol , vol.28 , pp. 5275-5287
    • Varghese, B.1    Barriere, H.2    Carbone, C.J.3    Banerjee, A.4    Swaminathan, G.5    Plotnikov, A.6
  • 30
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins. Getting in on the Akt
    • Brazil DP, Park J, Hemmings BA. PKB binding proteins. Getting in on the Akt. Cell 2002; 111:293-303.
    • (2002) Cell , vol.111 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 31
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC. The phosphoinositide 3-kinase pathway. Science 2002; 296:1655-7.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 32
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta SR, Brunet A, Greenberg ME. Cellular survival: a play in three Akts. Genes Dev 1999; 13:2905-27.
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 33
    • 69249208791 scopus 로고    scopus 로고
    • The Akt kinases: Isoform specificity in metabolism and cancer
    • Gonzalez E, McGraw TE. The Akt kinases: isoform specificity in metabolism and cancer. Cell Cycle 2009; 8:2502-8.
    • (2009) Cell Cycle , vol.8 , pp. 2502-2508
    • Gonzalez, E.1    McGraw, T.E.2
  • 34
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning BD, Cantley LC. AKT/PKB signaling: navigating downstream. Cell 2007; 129:1261-74.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 35
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin DA, Sabatini DM. Defining the role of mTOR in cancer. Cancer Cell 2007; 12:9-22.
    • (2007) Cancer Cell , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 36
    • 0032431032 scopus 로고    scopus 로고
    • The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway
    • Wu X, Senechal K, Neshat MS, Whang YE, Sawyers CL. The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway. Proc Natl Acad Sci USA 1998; 95:15587-91.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15587-15591
    • Wu, X.1    Senechal, K.2    Neshat, M.S.3    Whang, Y.E.4    Sawyers, C.L.5
  • 37
    • 0034681264 scopus 로고    scopus 로고
    • The multiple roles of PTEN in tumor suppression
    • Di Cristofano A, Pandolfi PP. The multiple roles of PTEN in tumor suppression. Cell 2000; 100:387-90.
    • (2000) Cell , vol.100 , pp. 387-390
    • Di Cristofano, A.1    Pandolfi, P.P.2
  • 38
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao R, Cooper GM. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science 1995; 267:2003-6.
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 39
    • 0033517189 scopus 로고    scopus 로고
    • NFkappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes ON, Mayo LD, Gustin JA, Pfeffer SR, Pfeffer LM, Donner DB. NFkappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 1999; 401:82-5.
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5    Donner, D.B.6
  • 40
    • 64049090611 scopus 로고    scopus 로고
    • Skp2: Caught in the Akt
    • Ecker K, Hengst L. Skp2: caught in the Akt. Nat Cell Biol 2009; 11:377-9.
    • (2009) Nat Cell Biol , vol.11 , pp. 377-379
    • Ecker, K.1    Hengst, L.2
  • 41
    • 64049086572 scopus 로고    scopus 로고
    • Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction
    • Gao D, Inuzuka H, Tseng A, Chin RY, Toker A, Wei W. Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction. Nat Cell Biol 2009; 11:397-408.
    • (2009) Nat Cell Biol , vol.11 , pp. 397-408
    • Gao, D.1    Inuzuka, H.2    Tseng, A.3    Chin, R.Y.4    Toker, A.5    Wei, W.6
  • 42
    • 64049087382 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB
    • Lin HK, Wang G, Chen Z, Teruya-Feldstein J, Liu Y, Chan CH, et al. Phosphorylation-dependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB. Nat Cell Biol 2009; 11:420-32.
    • (2009) Nat Cell Biol , vol.11 , pp. 420-432
    • Lin, H.K.1    Wang, G.2    Chen, Z.3    Teruya-Feldstein, J.4    Liu, Y.5    Chan, C.H.6
  • 43
    • 0036683093 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase
    • Lin HK, Wang L, Hu YC, Altuwaijri S, Chang C. Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase. EMBO J 2002; 21:4037-48.
    • (2002) EMBO J , vol.21 , pp. 4037-4048
    • Lin, H.K.1    Wang, L.2    Hu, Y.C.3    Altuwaijri, S.4    Chang, C.5
  • 44
    • 0035949588 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus
    • Mayo LD, Donner DB. A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus. Proc Natl Acad Sci USA 2001; 98:11598-603.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11598-11603
    • Mayo, L.D.1    Donner, D.B.2
  • 45
    • 0035736487 scopus 로고    scopus 로고
    • HER-2/neu induces p53 ubiquitination via Aktmediated MDM2 phosphorylation
    • Zhou BP, Liao Y, Xia W, Zou Y, Spohn B, Hung MC. HER-2/neu induces p53 ubiquitination via Aktmediated MDM2 phosphorylation. Nat Cell Biol 2001; 3:973-82.
    • (2001) Nat Cell Biol , vol.3 , pp. 973-982
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Zou, Y.4    Spohn, B.5    Hung, M.C.6
  • 48
    • 1842785189 scopus 로고    scopus 로고
    • Signaling by insulin-like growth factor 1 in brain
    • Bondy CA, Cheng CM. Signaling by insulin-like growth factor 1 in brain. Eur J Pharmacol 2004; 490:25-31.
    • (2004) Eur J Pharmacol , vol.490 , pp. 25-31
    • Bondy, C.A.1    Cheng, C.M.2
  • 49
    • 27644528406 scopus 로고    scopus 로고
    • Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration
    • Li J, Ballif BA, Powelka AM, Dai J, Gygi SP, Hsu VW. Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration. Dev Cell 2005; 9:663-73.
    • (2005) Dev Cell , vol.9 , pp. 663-673
    • Li, J.1    Ballif, B.A.2    Powelka, A.M.3    Dai, J.4    Gygi, S.P.5    Hsu, V.W.6
  • 51
    • 0242664130 scopus 로고    scopus 로고
    • Akt phosphorylation of serine 21 on Pak1 modulates Nck binding and cell migration
    • Zhou GL, Zhuo Y, King CC, Fryer BH, Bokoch GM, Field J. Akt phosphorylation of serine 21 on Pak1 modulates Nck binding and cell migration. Mol Cell Biol 2003; 23:8058-69.
    • (2003) Mol Cell Biol , vol.23 , pp. 8058-8069
    • Zhou, G.L.1    Zhuo, Y.2    King, C.C.3    Fryer, B.H.4    Bokoch, G.M.5    Field, J.6
  • 52
    • 0034455310 scopus 로고    scopus 로고
    • Overexpression of insulin-like growth factor binding protein-5 helps accelerate progression to androgen-independence in the human prostate LNCaP tumor model through activation of phosphatidylinositol 3′-kinase pathway
    • DOI 10.1210/en.141.6.2257
    • Miyake H, Nelson C, Rennie PS, Gleave ME. Overexpression of insulin-like growth factor binding protein-5 helps accelerate progression to androgenindependence in the human prostate LNCaP tumor model through activation of phosphatidylinositol 3′-kinase pathway. Endocrinology 2000; 141:2257-65. (Pubitemid 32274381)
    • (2000) Endocrinology , vol.141 , Issue.6 , pp. 2257-2265
    • Miyake, H.1    Nelson, C.2    Rennie, P.S.3    Gleave, M.E.4
  • 54
    • 0026667730 scopus 로고
    • AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas
    • Cheng JQ, Godwin AK, Bellacosa A, Taguchi T, Franke TF, Hamilton TC, et al. AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas. Proc Natl Acad Sci USA 1992; 89:9267-71.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9267-9271
    • Cheng, J.Q.1    Godwin, A.K.2    Bellacosa, A.3    Taguchi, T.4    Franke, T.F.5    Hamilton, T.C.6
  • 55
    • 0001457668 scopus 로고    scopus 로고
    • Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA
    • Cheng JQ, Ruggeri B, Klein WM, Sonoda G, Altomare DA, Watson DK, et al. Amplification of AKT2 in human pancreatic cells and inhibition of AKT2 expression and tumorigenicity by antisense RNA. Proc Natl Acad Sci USA 1996; 93:3636-41.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3636-3641
    • Cheng, J.Q.1    Ruggeri, B.2    Klein, W.M.3    Sonoda, G.4    Altomare, D.A.5    Watson, D.K.6
  • 56
    • 0001582482 scopus 로고
    • Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: Amplification of AKT1 in a primary human gastric adenocarcinoma
    • Staal SP. Molecular cloning of the akt oncogene and its human homologues AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc Natl Acad Sci USA 1987; 84:5034-7.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5034-5037
    • Staal, S.P.1
  • 59
    • 76649085239 scopus 로고    scopus 로고
    • AKT1 mutations in bladder cancer: Identification of a novel oncogenic mutation that can co-operate with E17K
    • Askham JM, Platt F, Chambers PA, Snowden H, Taylor CF, Knowles MA. AKT1 mutations in bladder cancer: identification of a novel oncogenic mutation that can co-operate with E17K. Oncogene 2009.
    • (2009) Oncogene
    • Askham, J.M.1    Platt, F.2    Chambers, P.A.3    Snowden, H.4    Taylor, C.F.5    Knowles, M.A.6
  • 60
  • 61
    • 43249115083 scopus 로고    scopus 로고
    • Mutational analysis of oncogenic AKT E17K mutation in common solid cancers and acute leukaemias
    • Kim MS, Jeong EG, Yoo NJ, Lee SH. Mutational analysis of oncogenic AKT E17K mutation in common solid cancers and acute leukaemias. Br J Cancer 2008; 98:1533-5.
    • (2008) Br J Cancer , vol.98 , pp. 1533-1535
    • Kim, M.S.1    Jeong, E.G.2    Yoo, N.J.3    Lee, S.H.4
  • 64
    • 67649868092 scopus 로고    scopus 로고
    • The oncogenic mutation in the pleckstrin homology domain of AKT1 in endometrial carcinomas
    • Shoji K, Oda K, Nakagawa S, Hosokawa S, Nagae G, Uehara Y, et al. The oncogenic mutation in the pleckstrin homology domain of AKT1 in endometrial carcinomas. Br J Cancer 2009; 101:145-8.
    • (2009) Br J Cancer , vol.101 , pp. 145-148
    • Shoji, K.1    Oda, K.2    Nakagawa, S.3    Hosokawa, S.4    Nagae, G.5    Uehara, Y.6
  • 69
    • 0038271762 scopus 로고    scopus 로고
    • Prostate intraepithelial neoplasia induced by prostate restricted Akt activation: The MPAKT model
    • Majumder PK, Yeh JJ, George DJ, Febbo PG, Kum J, Xue Q, et al. Prostate intraepithelial neoplasia induced by prostate restricted Akt activation: the MPAKT model. Proc Natl Acad Sci USA 2003; 100:7841-6.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7841-7846
    • Majumder, P.K.1    Yeh, J.J.2    George, D.J.3    Febbo, P.G.4    Kum, J.5    Xue, Q.6
  • 70
    • 53649106357 scopus 로고    scopus 로고
    • Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways
    • Bayascas JR. Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways. Cell Cycle 2008; 7:2978-82.
    • (2008) Cell Cycle , vol.7 , pp. 2978-2982
    • Bayascas, J.R.1
  • 72
    • 33747819801 scopus 로고    scopus 로고
    • mTOR and cancer: Insights into a complex relationship
    • Sabatini DM. mTOR and cancer: insights into a complex relationship. Nat Rev Cancer 2006; 6:729-34.
    • (2006) Nat Rev Cancer , vol.6 , pp. 729-734
    • Sabatini, D.M.1
  • 73
    • 27944448894 scopus 로고    scopus 로고
    • Involvement of PP2A in viral and cellular transformation
    • Arroyo JD, Hahn WC. Involvement of PP2A in viral and cellular transformation. Oncogene 2005; 24:7746-55.
    • (2005) Oncogene , vol.24 , pp. 7746-7755
    • Arroyo, J.D.1    Hahn, W.C.2
  • 74
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades by protein phosphatase 2A
    • DOI 10.1016/S0968-0004(99)01375-4, PII S0968000499013754
    • Millward TA, Zolnierowicz S, Hemmings BA. Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem Sci 1999; 24:186-91. (Pubitemid 29348452)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.5 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 75
    • 33947203621 scopus 로고    scopus 로고
    • PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms
    • Brognard J, Sierecki E, Gao T, Newton AC. PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. Mol Cell 2007; 25:917-31.
    • (2007) Mol Cell , vol.25 , pp. 917-931
    • Brognard, J.1    Sierecki, E.2    Gao, T.3    Newton, A.C.4
  • 76
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis and suppresses tumor growth
    • Gao T, Furnari F, Newton AC. PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis and suppresses tumor growth. Mol Cell 2005; 18:13-24.
    • (2005) Mol Cell , vol.18 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 77
    • 33947243276 scopus 로고    scopus 로고
    • PHLPPing it off: Phosphatases get in the Akt
    • Mendoza MC, Blenis J. PHLPPing it off: phosphatases get in the Akt. Mol Cell 2007; 25:798-800.
    • (2007) Mol Cell , vol.25 , pp. 798-800
    • Mendoza, M.C.1    Blenis, J.2
  • 78
    • 69249228672 scopus 로고    scopus 로고
    • FKBP51 affects cancer cell response to chemotherapy by negatively regulating Akt
    • Pei H, Li L, Fridley BL, Jenkins GD, Kalari KR, Lingle W, et al. FKBP51 affects cancer cell response to chemotherapy by negatively regulating Akt. Cancer Cell 2009; 16:259-66.
    • (2009) Cancer Cell , vol.16 , pp. 259-266
    • Pei, H.1    Li, L.2    Fridley, B.L.3    Jenkins, G.D.4    Kalari, K.R.5    Lingle, W.6
  • 80
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • Beaulieu JM, Sotnikova TD, Marion S, Lefkowitz RJ, Gainetdinov RR, Caron MG. An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 2005; 122:261-73.
    • (2005) Cell , vol.122 , pp. 261-273
    • Beaulieu, J.M.1    Sotnikova, T.D.2    Marion, S.3    Lefkowitz, R.J.4    Gainetdinov, R.R.5    Caron, M.G.6
  • 81
    • 61349130027 scopus 로고    scopus 로고
    • Deficiency of a beta-arrestin-2 signal complex contributes to insulin resistance
    • Luan B, Zhao J, Wu H, Duan B, Shu G, Wang X, et al. Deficiency of a beta-arrestin-2 signal complex contributes to insulin resistance. Nature 2009; 457:1146-9.
    • (2009) Nature , vol.457 , pp. 1146-1149
    • Luan, B.1    Zhao, J.2    Wu, H.3    Duan, B.4    Shu, G.5    Wang, X.6
  • 83
    • 0029807471 scopus 로고    scopus 로고
    • Akt is a direct target of the phosphatidylinositol 3-kinase. Activation by growth factors, v-src and v-Ha-ras, in Sf9 and mammalian cells
    • Datta K, Bellacosa A, Chan TO, Tsichlis PN. Akt is a direct target of the phosphatidylinositol 3-kinase. Activation by growth factors, v-src and v-Ha-ras, in Sf9 and mammalian cells. J Biol Chem 1996; 271:30835-9.
    • (1996) J Biol Chem , vol.271 , pp. 30835-30839
    • Datta, K.1    Bellacosa, A.2    Chan, T.O.3    Tsichlis, P.N.4
  • 84
    • 0037938847 scopus 로고    scopus 로고
    • Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation
    • DOI 10.1074/jbc.M212525200
    • Jiang T, Qiu Y. Interaction between Src and a C-terminal proline-rich motif of Akt is required for Akt activation. J Biol Chem 2003; 278:15789-93. (Pubitemid 36799692)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 15789-15793
    • Jiang, T.1    Qiu, Y.2
  • 85
    • 0033393957 scopus 로고    scopus 로고
    • TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src
    • Wong BR, Besser D, Kim N, Arron JR, Vologodskaia M, Hanafusa H, et al. TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src. Mol Cell 1999; 4:1041-9.
    • (1999) Mol Cell , vol.4 , pp. 1041-1049
    • Wong, B.R.1    Besser, D.2    Kim, N.3    Arron, J.R.4    Vologodskaia, M.5    Hanafusa, H.6
  • 86
    • 69549122045 scopus 로고    scopus 로고
    • Cell signaling. Blocking Akt-ivity
    • Restuccia DF, Hemmings BA. Cell signaling. Blocking Akt-ivity. Science 2009; 325:1083-4.
    • (2009) Science , vol.325 , pp. 1083-1084
    • Restuccia, D.F.1    Hemmings, B.A.2
  • 87
    • 34247116441 scopus 로고    scopus 로고
    • Physiological roles of PKB/Akt isoforms in development and disease
    • DOI 10.1042/BST0350231
    • Dummler B, Hemmings BA. Physiological roles of PKB/Akt isoforms in development and disease. Biochem Soc Trans 2007; 35:231-5. (Pubitemid 46596476)
    • (2007) Biochemical Society Transactions , vol.35 , Issue.2 , pp. 231-235
    • Dummler, B.1    Hemmings, B.A.2
  • 88
    • 29144488505 scopus 로고    scopus 로고
    • Distinct roles of Akt1 and Akt2 in regulating cell migration and epithelial-mesenchymal transition
    • Irie HY, Pearline RV, Grueneberg D, Hsia M, Ravichandran P, Kothari N, et al. Distinct roles of Akt1 and Akt2 in regulating cell migration and epithelial-mesenchymal transition. J Cell Biol 2005; 171:1023-34.
    • (2005) J Cell Biol , vol.171 , pp. 1023-1034
    • Irie, H.Y.1    Pearline, R.V.2    Grueneberg, D.3    Hsia, M.4    Ravichandran, P.5    Kothari, N.6
  • 89
  • 92
    • 0042030924 scopus 로고    scopus 로고
    • JNK-interacting protein 1 promotes Akt1 activation
    • Kim AH, Sasaki T, Chao MV. JNK-interacting protein 1 promotes Akt1 activation. J Biol Chem 2003; 278:29830-6.
    • (2003) J Biol Chem , vol.278 , pp. 29830-29836
    • Kim, A.H.1    Sasaki, T.2    Chao, M.V.3
  • 93
    • 34547795824 scopus 로고    scopus 로고
    • Proto-oncogene TCL1: More than just a coactivator for Akt
    • Noguchi M, Ropars V, Roumestand C, Suizu F. Proto-oncogene TCL1: more than just a coactivator for Akt. Faseb J 2007; 21:2273-84.
    • (2007) Faseb J , vol.21 , pp. 2273-2284
    • Noguchi, M.1    Ropars, V.2    Roumestand, C.3    Suizu, F.4
  • 94
    • 27844469655 scopus 로고    scopus 로고
    • Selective cellular effects of over-expressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners
    • Varnai P, Bondeva T, Tamas P, Toth B, Buday L, Hunyady L, et al. Selective cellular effects of over-expressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners. J Cell Sci 2005; 118:4879-88.
    • (2005) J Cell Sci , vol.118 , pp. 4879-4888
    • Varnai, P.1    Bondeva, T.2    Tamas, P.3    Toth, B.4    Buday, L.5    Hunyady, L.6
  • 97
    • 55549119209 scopus 로고    scopus 로고
    • Scaffolding function of PAK in the PDK1-Akt pathway
    • Higuchi M, Onishi K, Kikuchi C, Gotoh Y. Scaffolding function of PAK in the PDK1-Akt pathway. Nat Cell Biol 2008; 10:1356-64.
    • (2008) Nat Cell Biol , vol.10 , pp. 1356-1364
    • Higuchi, M.1    Onishi, K.2    Kikuchi, C.3    Gotoh, Y.4
  • 98
    • 53349164136 scopus 로고    scopus 로고
    • The type I TGFbeta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner
    • Sorrentino A, Thakur N, Grimsby S, Marcusson A, von Bulow V, Schuster N, et al. The type I TGFbeta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner. Nat Cell Biol 2008; 10:1199-207.
    • (2008) Nat Cell Biol , vol.10 , pp. 1199-1207
    • Sorrentino, A.1    Thakur, N.2    Grimsby, S.3    Marcusson, A.4    Von Bulow, V.5    Schuster, N.6
  • 99
    • 52049111663 scopus 로고    scopus 로고
    • TRAF6 mediates Smad-independent activation of JNK and p38 by TGFbeta
    • Yamashita M, Fatyol K, Jin C, Wang X, Liu Z, Zhang YE. TRAF6 mediates Smad-independent activation of JNK and p38 by TGFbeta. Mol Cell 2008; 31:918-24.
    • (2008) Mol Cell , vol.31 , pp. 918-924
    • Yamashita, M.1    Fatyol, K.2    Jin, C.3    Wang, X.4    Liu, Z.5    Zhang, Y.E.6
  • 100
    • 77950367657 scopus 로고    scopus 로고
    • Two mechanistically and temporally distinct NFkappaB activation pathways in IL-1 signaling
    • Yamazaki K, Gohda J, Kanayama A, Miyamoto Y, Sakurai H, Yamamoto M, et al. Two mechanistically and temporally distinct NFkappaB activation pathways in IL-1 signaling. Sci Signal 2009; 2:66.
    • (2009) Sci Signal , vol.2 , pp. 66
    • Yamazaki, K.1    Gohda, J.2    Kanayama, A.3    Miyamoto, Y.4    Sakurai, H.5    Yamamoto, M.6
  • 101
    • 69049108580 scopus 로고    scopus 로고
    • Cytokine-induced activation of mixed lineage kinase 3 requires TRAF2 and TRAF6
    • Korchnak AC, Zhan Y, Aguilar MT, Chadee DN. Cytokine-induced activation of mixed lineage kinase 3 requires TRAF2 and TRAF6. Cell Signal 2009; 21:1620-5.
    • (2009) Cell Signal , vol.21 , pp. 1620-1625
    • Korchnak, A.C.1    Zhan, Y.2    Aguilar, M.T.3    Chadee, D.N.4
  • 103
    • 0034693754 scopus 로고    scopus 로고
    • Signaling network of the Btk family kinases
    • Qiu Y, Kung HJ. Signaling network of the Btk family kinases. Oncogene 2000; 19:5651-61.
    • (2000) Oncogene , vol.19 , pp. 5651-5661
    • Qiu, Y.1    Kung, H.J.2
  • 104
    • 58149178554 scopus 로고    scopus 로고
    • TRAF6 autoubiquitination-independent activation of the NFkappaB and MAPK pathways in response to IL-1 and RANKL
    • Walsh MC, Kim GK, Maurizio PL, Molnar EE, Choi Y. TRAF6 autoubiquitination-independent activation of the NFkappaB and MAPK pathways in response to IL-1 and RANKL. PLoS One 2008; 3:4064.
    • (2008) PLoS One , vol.3 , pp. 4064
    • Walsh, M.C.1    Kim, G.K.2    Maurizio, P.L.3    Molnar, E.E.4    Choi, Y.5
  • 105
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia ZP, Sun L, Chen X, Pineda G, Jiang X, Adhikari A, et al. Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 2009; 461:114-9.
    • (2009) Nature , vol.461 , pp. 114-119
    • Xia, Z.P.1    Sun, L.2    Chen, X.3    Pineda, G.4    Jiang, X.5    Adhikari, A.6
  • 106
    • 0033561039 scopus 로고    scopus 로고
    • TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40 and LPS signaling
    • Lomaga MA, Yeh WC, Sarosi I, Duncan GS, Furlonger C, Ho A, et al. TRAF6 deficiency results in osteopetrosis and defective interleukin-1, CD40 and LPS signaling. Genes Dev 1999; 13:1015-24.
    • (1999) Genes Dev , vol.13 , pp. 1015-1024
    • Lomaga, M.A.1    Yeh, W.C.2    Sarosi, I.3    Duncan, G.S.4    Furlonger, C.5    Ho, A.6
  • 107
    • 63749105896 scopus 로고    scopus 로고
    • Mechanism of TGFbeta signaling to growth arrest, apoptosis and epithelial-mesenchymal transition
    • Heldin CH, Landstrom M, Moustakas A. Mechanism of TGFbeta signaling to growth arrest, apoptosis and epithelial-mesenchymal transition. Curr Opin Cell Biol 2009; 21:166-76.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 166-176
    • Heldin, C.H.1    Landstrom, M.2    Moustakas, A.3
  • 108
    • 0036882836 scopus 로고    scopus 로고
    • IL-1beta-induced phosphorylation of PKB/Akt depends on the presence of IRAK-1
    • DOI 10.1002/1521-4141(200212)32:12<3689::AID-IMMU3689>3.0.CO;2-X
    • Neumann D, Lienenklaus S, Rosati O, Martin MU. IL-1beta-induced phosphorylation of PKB/Akt depends on the presence of IRAK-1. Eur J Immunol 2002; 32:3689-98. (Pubitemid 36024405)
    • (2002) European Journal of Immunology , vol.32 , Issue.12 , pp. 3689-3698
    • Neumann, D.1    Lienenklaus, S.2    Rosati, O.3    Martin, M.U.4
  • 109
    • 3543097542 scopus 로고    scopus 로고
    • RIP links TLR4 to Akt and is essential for cell survival in response to LPS stimulation
    • Vivarelli MS, McDonald D, Miller M, Cusson N, Kelliher M, Geha RS. RIP links TLR4 to Akt and is essential for cell survival in response to LPS stimulation. J Exp Med 2004; 200:399-404.
    • (2004) J Exp Med , vol.200 , pp. 399-404
    • Vivarelli, M.S.1    McDonald, D.2    Miller, M.3    Cusson, N.4    Kelliher, M.5    Geha, R.S.6
  • 110
    • 2942537700 scopus 로고    scopus 로고
    • Lipopolysaccharide initiates a TRAF6-mediated endothelial survival signal
    • DOI 10.1182/blood-2003-06-2118
    • Wong F, Hull C, Zhande R, Law J, Karsan A. Lipopolysaccharide initiates a TRAF6-mediated endothelial survival signal. Blood 2004; 103:4520-6. (Pubitemid 38745979)
    • (2004) Blood , vol.103 , Issue.12 , pp. 4520-4526
    • Wong, F.1    Hull, C.2    Zhande, R.3    Law, J.4    Karsan, A.5
  • 111
    • 58149202128 scopus 로고    scopus 로고
    • Is NFkappaB a good target for cancer therapy? Hopes and pitfalls
    • Baud V, Karin M. Is NFkappaB a good target for cancer therapy? Hopes and pitfalls. Nat Rev Drug Discov 2009; 8:33-40.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 33-40
    • Baud, V.1    Karin, M.2
  • 112
    • 38049054248 scopus 로고    scopus 로고
    • Updates on p53: Modulation of p53 degradation as a therapeutic approach
    • Dey A, Verma CS, Lane DP. Updates on p53: modulation of p53 degradation as a therapeutic approach. Br J Cancer 2008; 98:4-8.
    • (2008) Br J Cancer , vol.98 , pp. 4-8
    • Dey, A.1    Verma, C.S.2    Lane, D.P.3
  • 113
    • 33846692198 scopus 로고    scopus 로고
    • Signal integration and diversification through the p62 scaffold protein
    • DOI 10.1016/j.tibs.2006.12.002, PII S0968000406003276
    • Moscat J, Diaz-Meco MT, Wooten MW. Signal integration and diversification through the p62 scaffold protein. Trends Biochem Sci 2007; 32:95-100. (Pubitemid 46199192)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.2 , pp. 95-100
    • Moscat, J.1    Diaz-Meco, M.T.2    Wooten, M.W.3
  • 114
    • 41249084239 scopus 로고    scopus 로고
    • The Signaling Adaptor p62 Is an Important NF-kappaB Mediator in Tumorigenesis
    • DOI 10.1016/j.ccr.2008.02.001, PII S1535610808000421
    • Duran A, Linares JF, Galvez AS, Wikenheiser K, Flores JM, Diaz-Meco MT, et al. The signaling adaptor p62 is an important NFkappaB mediator in tumorigenesis. Cancer Cell 2008; 13:343-54. (Pubitemid 351446193)
    • (2008) Cancer Cell , vol.13 , Issue.4 , pp. 343-354
    • Duran, A.1    Linares, J.F.2    Galvez, A.S.3    Wikenheiser, K.4    Flores, J.M.5    Diaz-Meco, M.T.6    Moscat, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.