메뉴 건너뛰기




Volumn 288, Issue 3, 2013, Pages 1674-1684

Ubiquitin-dependent regulation of phospho-AKT Dynamics by the ubiquitin E3 LIGASE, NEDD4-1, in the insulin-like growth factor-1 response

Author keywords

[No Author keywords available]

Indexed keywords

AKT ACTIVATION; CELLULAR PROCESS; CHAIN FORMATION; E3 LIGASE; IN-VITRO; IN-VIVO; INSULIN-LIKE GROWTH FACTOR; INSULIN-LIKE GROWTH FACTOR-1; LIGASES; MEMBRANE BINDING; PERINUCLEAR REGION; POLYUBIQUITIN; PROTEASOMAL DEGRADATION; SUBCELLULAR LOCALIZATIONS; UBIQUITIN; UBIQUITINATION;

EID: 84872736566     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.416339     Document Type: Article
Times cited : (93)

References (34)
  • 1
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., Yang, S.-I., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., and Tsichlis, P. N. (1995) The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81, 727-736
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.-I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 2
    • 23944526062 scopus 로고    scopus 로고
    • Activation of AKT kinases in cancer: Implications for therapeutic targeting
    • DOI 10.1016/S0065-230X(05)94002-5, PII S0065230X05940025
    • Bellacosa, A., Kumar, C. C., Cristofano, A. D., Testa, J. R., George, F. V., and George, K. (2005) Activation of AKT kinases in cancer. Implications for therapeutic targeting. Adv. Cancer Res. 94, 29-86 (Pubitemid 41202364)
    • (2005) Advances in Cancer Research , vol.94 , Issue.1 SUPPL. , pp. 29-86
    • Bellacosa, A.1    Kumar, C.C.2    Cristofano, A.D.3    Testa, J.R.4
  • 3
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling. Navigating downstream
    • Manning, B. D., and Cantley, L. C. (2007) AKT/PKB signaling. Navigating downstream. Cell 129, 1261-1274
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 4
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • DOI 10.1126/science.1106148
    • Sarbassov, D. D., Guertin, D. A., Ali, S. M., and Sabatini, D. M. (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101 (Pubitemid 40262113)
    • (2005) Science , vol.307 , Issue.5712 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 5
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • DOI 10.1016/j.molcel.2005.03.008
    • Gao, T., Furnari, F., and Newton, A. C. (2005) PHLPP. A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol. Cell 18, 13-24 (Pubitemid 40444644)
    • (2005) Molecular Cell , vol.18 , Issue.1 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 6
    • 33947203621 scopus 로고    scopus 로고
    • PHLPP and a Second Isoform, PHLPP2, Differentially Attenuate the Amplitude of Akt Signaling by Regulating Distinct Akt Isoforms
    • DOI 10.1016/j.molcel.2007.02.017, PII S1097276507001177
    • Brognard, J., Sierecki, E., Gao, T., and Newton, A. C. (2007) PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. Mol. Cell 25, 917-931 (Pubitemid 46436532)
    • (2007) Molecular Cell , vol.25 , Issue.6 , pp. 917-931
    • Brognard, J.1    Sierecki, E.2    Gao, T.3    Newton, A.C.4
  • 7
    • 0345381737 scopus 로고    scopus 로고
    • The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor
    • DOI 10.1128/MCB.23.9.3363-3372.2003
    • Vecchione, A., Marchese, A., Henry, P., Rotin, D., and Morrione, A. (2003) The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor. Mol. Cell Biol. 23, 3363-3372 (Pubitemid 36459247)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.9 , pp. 3363-3372
    • Vecchione, A.1    Marchese, A.2    Henry, P.3    Rotin, D.4    Morrione, A.5
  • 13
    • 77951234781 scopus 로고    scopus 로고
    • Ubiquitination of PTEN (phosphatase and tensin homolog) inhibits phosphatase activity and is enhanced by membrane targeting and hyperosmotic stress
    • Maccario, H., Perera, N. M., Gray, A., Downes, C. P., and Leslie, N. R. (2010) Ubiquitination of PTEN (phosphatase and tensin homolog) inhibits phosphatase activity and is enhanced by membrane targeting and hyperosmotic stress. J. Biol. Chem. 285, 12620-12628
    • (2010) J. Biol. Chem. , vol.285 , pp. 12620-12628
    • MacCario, H.1    Perera, N.M.2    Gray, A.3    Downes, C.P.4    Leslie, N.R.5
  • 14
    • 49149117504 scopus 로고    scopus 로고
    • Crucial role of theCterminus of PTEN in antagonizing NEDD4-1-mediated PTEN ubiquitination and degradation
    • Wang, X., Shi, Y., Wang, J., Huang, G., and Jiang, X. (2008) Crucial role of theCterminus of PTEN in antagonizing NEDD4-1-mediated PTEN ubiquitination and degradation. Biochem. J. 414, 221-229
    • (2008) Biochem. J. , vol.414 , pp. 221-229
    • Wang, X.1    Shi, Y.2    Wang, J.3    Huang, G.4    Jiang, X.5
  • 15
  • 19
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the α domain
    • DOI 10.1016/S0092-8674(94)90502-9
    • Treier, M., Staszewski, L. M., and Bohmann, D. (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78, 787-798 (Pubitemid 24294454)
    • (1994) Cell , vol.78 , Issue.5 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 20
    • 33748794547 scopus 로고    scopus 로고
    • Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies
    • Chou, T. C. (2006) Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies. Pharmacol. Rev. 58, 621-681
    • (2006) Pharmacol. Rev. , vol.58 , pp. 621-681
    • Chou, T.C.1
  • 21
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • DOI 10.1126/science.275.5300.665
    • Franke, T. F., Kaplan, D. R., Cantley, L. C., and Toker, A. (1997) Direct regulation of the Akt proto-oncogene product by phosphatidylinositol 3,4-bisphosphate. Science 275, 665-668 (Pubitemid 27061333)
    • (1997) Science , vol.275 , Issue.5300 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 23
    • 79954600448 scopus 로고    scopus 로고
    • MTOR complex 2 targets Akt for proteasomal degradation via phosphorylation at the hydrophobic motif
    • Wu, Y. T., Ouyang, W., Lazorchak, A. S., Liu, D., Shen, H. M., and Su, B. (2011) mTOR complex 2 targets Akt for proteasomal degradation via phosphorylation at the hydrophobic motif. J. Biol. Chem. 286, 14190-14198
    • (2011) J. Biol. Chem. , vol.286 , pp. 14190-14198
    • Wu, Y.T.1    Ouyang, W.2    Lazorchak, A.S.3    Liu, D.4    Shen, H.M.5    Su, B.6
  • 29
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • DOI 10.1074/jbc.M206322200
    • Basso, A. D., Solit, D. B., Chiosis, G., Giri, B., Tsichlis, P., and Rosen, N. (2002) Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. 277, 39858-39866 (Pubitemid 35190971)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 30
    • 0030727172 scopus 로고    scopus 로고
    • Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bβ
    • DOI 10.1074/jbc.272.48.30491
    • Meier, R., Alessi, D. R., Cron, P., Andjelković, M., and Hemmings, B. A. (1997) Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bα. J. Biol. Chem. 272, 30491-30497 (Pubitemid 27512261)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.48 , pp. 30491-30497
    • Meier, R.1    Alessi, D.R.2    Cron, P.3    Andjelkovic, M.4    Hemmings, B.A.5
  • 33
    • 33745316089 scopus 로고    scopus 로고
    • Identification of a tumour suppressor network opposing nuclear Akt function
    • DOI 10.1038/nature04809, PII NATURE04809
    • Trotman, L. C., Alimonti, A., Scaglioni, P. P., Koutcher, J. A., Cordon-Cardo, C., and Pandolfi, P. P. (2006) Identification of a tumour suppressor network opposing nuclear Akt function. Nature 441, 523-527 (Pubitemid 44050155)
    • (2006) Nature , vol.441 , Issue.7092 , pp. 523-527
    • Trotman, L.C.1    Alimonti, A.2    Scaglioni, P.P.3    Koutcher, J.A.4    Cordon-Cardo, C.5    Pandolfi, P.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.