메뉴 건너뛰기




Volumn 289, Issue 36, 2014, Pages 25227-25240

Akt-dependent activation of mTORC1 complex involves phosphorylation of mTOR (mammalian target of rapamycin) by IκB kinase α (IKKα)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL CULTURE; CHEMICAL ACTIVATION; ENZYMES; MAMMALS; PHOSPHORYLATION;

EID: 84906971768     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.554881     Document Type: Article
Times cited : (123)

References (58)
  • 1
    • 78650510609 scopus 로고    scopus 로고
    • mTOR: From growth signal integration to cancer, diabetes, and ageing
    • Zoncu, R., Efeyan, A., and Sabatini, D. M. (2011) mTOR: from growth signal integration to cancer, diabetes, and ageing. Nat. Rev. Mol. Cell Biol. 12, 21-35
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 2
    • 79952104568 scopus 로고    scopus 로고
    • mTOR couples cellular nutrient sensing to organismal metabolic homeostasis
    • Howell, J. J., and Manning, B. D. (2011) mTOR couples cellular nutrient sensing to organismal metabolic homeostasis. Trends Endocrinol. Metab. 22, 94-102
    • (2011) Trends Endocrinol. Metab. , vol.22 , pp. 94-102
    • Howell, J.J.1    Manning, B.D.2
  • 3
    • 84862908818 scopus 로고    scopus 로고
    • AMPK and mTOR in cellular energy homeostasis and drug targets
    • Inoki, K., Kim, J., and Guan, K.-L. (2012) AMPK and mTOR in cellular energy homeostasis and drug targets. Annu. Rev. Pharmacol. Toxicol. 52, 381-400
    • (2012) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 381-400
    • Inoki, K.1    Kim, J.2    Guan, K.-L.3
  • 4
    • 84884676252 scopus 로고    scopus 로고
    • Nutrient signaling to mTOR and cell growth
    • Jewell, J. L., Guan, K. L. (2013) Nutrient signaling to mTOR and cell growth. Trends Biochem. Sci. 38, 233-242
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 233-242
    • Jewell, J.L.1    Guan, K.L.2
  • 5
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • Ma, X. M., and Blenis, J. (2009) Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. Mol. Cell Biol. 10, 307-318
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 6
    • 79958064675 scopus 로고    scopus 로고
    • mTOR phosphorylates IMP2 to promote IGF2 mRNA translation by internal ribosomal entry
    • Dai, N., Rapley, J., Angel, M., Yanik, M. F., Blower, M. D., and Avruch, J. (2011) mTOR phosphorylates IMP2 to promote IGF2 mRNA translation by internal ribosomal entry. Genes Dev. 25, 1159-1172
    • (2011) Genes Dev. , vol.25 , pp. 1159-1172
    • Dai, N.1    Rapley, J.2    Angel, M.3    Yanik, M.F.4    Blower, M.D.5    Avruch, J.6
  • 7
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim, J., Kundu, M., Viollet, B., and Guan, K. L. (2011) AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 13, 132-141
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 8
    • 70449900928 scopus 로고    scopus 로고
    • TOR complex 2: A signaling pathway of its own
    • Cybulski N, Hall M. N. (2009) TOR complex 2: a signaling pathway of its own. Trends Biochem. Sci. 34, 620-627
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 620-627
    • Cybulski, N.1    Hall, M.N.2
  • 9
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • 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
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 10
    • 58649092475 scopus 로고    scopus 로고
    • mTORC2 controls hydrophobic motif phosphorylation and activation of SGK1
    • García-Martínez, J. M., and Alessi, D. R. (2008) mTORC2 controls hydrophobic motif phosphorylation and activation of SGK1. Biochem. J. 416, 375-385
    • (2008) Biochem. J. , vol.416 , pp. 375-385
    • García-Martínez, J.M.1    Alessi, D.R.2
  • 11
    • 58949084058 scopus 로고    scopus 로고
    • mTORC2 is the hydrophobic motif kinase for SGK1
    • Yan, L., Mieulet, V., and Lamb, R. (2008) mTORC2 is the hydrophobic motif kinase for SGK1. Biochem. J. 416, e19-e21
    • (2008) Biochem. J. , vol.416 , pp. e19-e21
    • Yan, L.1    Mieulet, V.2    Lamb, R.3
  • 13
    • 33745307617 scopus 로고    scopus 로고
    • Ras, PI3K, and mTOR signaling controls tumor growth
    • Shaw, R. J., and Cantley, L. C. (2006) Ras, PI3K, and mTOR signaling controls tumor growth. Nature 441, 424-430
    • (2006) Nature , vol.441 , pp. 424-430
    • Shaw, R.J.1    Cantley, L.C.2
  • 14
    • 33749447286 scopus 로고    scopus 로고
    • Akt and cancer: Is it all mTOR?
    • Rosen, N., and She, Q. B. (2006) Akt and cancer: is it all mTOR? Cancer Cell 10, 254-256
    • (2006) Cancer Cell , vol.10 , pp. 254-256
    • Rosen, N.1    She, Q.B.2
  • 15
    • 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
  • 16
    • 34047095297 scopus 로고    scopus 로고
    • The two TORCs and Akt
    • Bhaskar, P. T., and Hay, N. (2007) The two TORCs and Akt. Dev. Cell 12, 487-502
    • (2007) Dev. Cell , vol.12 , pp. 487-502
    • Bhaskar, P.T.1    Hay, N.2
  • 17
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the TSC2 tumor suppressor gene product tuberin as a target of the PI3K/Akt pathway
    • Manning, B. D., Tee, A. R., Logsdon, M. N., Blenis, J., and Cantley, L. C. (2002) Identification of the TSC2 tumor suppressor gene product tuberin as a target of the PI3K/Akt pathway. Mol. Cell 10, 151-162
    • (2002) Mol. Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5
  • 18
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signaling
    • Inoki, K., Li, Y., Zhu, T., Wu, J., and Guan, K.-L. (2002) TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signaling. Nat. Cell Biol. 4, 648-657
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.-L.5
  • 19
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumor suppressor proteins
    • Zhang, Y., Gao, X., Saucedo, L. J., Ru, B., Edgar, B. A., and Pan, D. (2003) Rheb is a direct target of the tuberous sclerosis tumor suppressor proteins. Nat. Cell Biol. 5, 578-581
    • (2003) Nat. Cell Biol. , vol.5 , pp. 578-581
    • Zhang, Y.1    Gao, X.2    Saucedo, L.J.3    Ru, B.4    Edgar, B.A.5    Pan, D.6
  • 21
    • 59749090661 scopus 로고    scopus 로고
    • Activation of mTORC1 in two steps: Rheb-GTP activation of catalytic function and increased binding of substrates to Raptor
    • Avruch, J., Long, X., Lin, Y., Ortiz-Vega, S., Rapley, J., Papageorgiou, A., Oshiro, N., and Kikkawa, U. (2009) Activation of mTORC1 in two steps: Rheb-GTP activation of catalytic function and increased binding of substrates to Raptor. Biochem. Soc. Trans. 37, 223-226
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 223-226
    • Avruch, J.1    Long, X.2    Lin, Y.3    Ortiz-Vega, S.4    Rapley, J.5    Papageorgiou, A.6    Oshiro, N.7    Kikkawa, U.8
  • 24
    • 34547099855 scopus 로고    scopus 로고
    • PRAS40 regulates mTORC1 kinase activity by functioning as a director inhibitor of substrate binding
    • Wang, L., Harris, T. E., Roth, R. A., and Lawrence, J. C. (2007) PRAS40 regulates mTORC1 kinase activity by functioning as a director inhibitor of substrate binding. J. Biol. Chem. 282, 20036-20044
    • (2007) J. Biol. Chem. , vol.282 , pp. 20036-20044
    • Wang, L.1    Harris, T.E.2    Roth, R.A.3    Lawrence, J.C.4
  • 25
    • 33745298519 scopus 로고    scopus 로고
    • Nuclear factor-κB in cancer development and progression
    • Karin, M. (2006) Nuclear factor-κB in cancer development and progression. Nature 441, 431-436
    • (2006) Nature , vol.441 , pp. 431-436
    • Karin, M.1
  • 27
    • 80052014052 scopus 로고    scopus 로고
    • Inflammation meets cancer, with NF-κB as the matchmaker
    • Ben-Neriah, Y., and Karin, M. (2011) Inflammation meets cancer, with NF-κB as the matchmaker. Nat. Immunol. 12, 715-723
    • (2011) Nat. Immunol. , vol.12 , pp. 715-723
    • Ben-Neriah, Y.1    Karin, M.2
  • 28
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century: Remarkable progress and outstanding questions
    • Hayden, M. S., and Ghosh, S. (2012) NF-κB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev. 26, 203-234
    • (2012) Genes Dev. , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 29
    • 84856213846 scopus 로고    scopus 로고
    • The diverse and complex roles of NF-κB subunits in cancer
    • Perkins, N. D. (2012) The diverse and complex roles of NF-κB subunits in cancer. Nat. Rev. Cancer. 12, 121-132
    • (2012) Nat. Rev. Cancer. , vol.12 , pp. 121-132
    • Perkins, N.D.1
  • 30
    • 84858726313 scopus 로고    scopus 로고
    • Regulation of cell death and autophagy by IKK and NF-κB: Critical mechanisms in immune function and cancer
    • Baldwin, A. S. (2012) Regulation of cell death and autophagy by IKK and NF-κB: critical mechanisms in immune function and cancer. Immunol. Rev. 246, 327-345
    • (2012) Immunol. Rev. , vol.246 , pp. 327-345
    • Baldwin, A.S.1
  • 32
    • 34047248402 scopus 로고    scopus 로고
    • Phosphorylation of CBP by IKKα promotes cell growth by switching the binding preference of CBP from p53 to NF-κB
    • Huang, W. C., Ju, T. K., Hung, M. C., and Chen, C. C. (2007) Phosphorylation of CBP by IKKα promotes cell growth by switching the binding preference of CBP from p53 to NF-κB. Mol. Cell 26, 75-87
    • (2007) Mol. Cell , vol.26 , pp. 75-87
    • Huang, W.C.1    Ju, T.K.2    Hung, M.C.3    Chen, C.C.4
  • 33
    • 35648958721 scopus 로고    scopus 로고
    • IκB kinase β phosphorylates the K63 deubiquitinase A20 to cause feedback inhibition of the NF-κB pathway
    • Hutti, J. E., Turk, B. E., Asara, J. M., Ma, A., Cantley, L. C., and Abbott, D. W. (2007) IκB kinase β phosphorylates the K63 deubiquitinase A20 to cause feedback inhibition of the NF-κB pathway. Mol. Cell. Biol. 27, 7451-7461
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7451-7461
    • Hutti, J.E.1    Turk, B.E.2    Asara, J.M.3    Ma, A.4    Cantley, L.C.5    Abbott, D.W.6
  • 34
    • 84859023600 scopus 로고    scopus 로고
    • p85α SH2 domain phosphorylation by IKK promotes feedback inhibition of PI3K and Akt in response to cellular starvation
    • Comb, W. C., Hutti, J. E., Cogswell, P., Cantley, L. C., and Baldwin, A. S. (2012) p85α SH2 domain phosphorylation by IKK promotes feedback inhibition of PI3K and Akt in response to cellular starvation. Mol. Cell 45, 719-730
    • (2012) Mol. Cell , vol.45 , pp. 719-730
    • Comb, W.C.1    Hutti, J.E.2    Cogswell, P.3    Cantley, L.C.4    Baldwin, A.S.5
  • 37
    • 34447131534 scopus 로고    scopus 로고
    • Regulation of mammalian target of rapamycin activity in PTEN-inactive prostate cancer cells by IKKα
    • Dan, H. C., Adli, M., and Baldwin, A. S. (2007) Regulation of mammalian target of rapamycin activity in PTEN-inactive prostate cancer cells by IKKα. Cancer Res. 67, 6263-6269
    • (2007) Cancer Res. , vol.67 , pp. 6263-6269
    • Dan, H.C.1    Adli, M.2    Baldwin, A.S.3
  • 38
    • 44849117768 scopus 로고    scopus 로고
    • Akt-dependent regulation of NF-κB is controlled by mTOR and Raptor in association with IKK
    • Dan, H. C., Cooper, M. J., Cogswell, P. C., Duncan, J. A., Ting, J. P., and Baldwin, A. S. (2008) Akt-dependent regulation of NF-κB is controlled by mTOR and Raptor in association with IKK. Genes Dev. 22, 1490-1500
    • (2008) Genes Dev. , vol.22 , pp. 1490-1500
    • Dan, H.C.1    Cooper, M.J.2    Cogswell, P.C.3    Duncan, J.A.4    Ting, J.P.5    Baldwin, A.S.6
  • 39
    • 47249125723 scopus 로고    scopus 로고
    • Differential involvement of IKKα and -β in cytokine- and insulin-induced mammalian target of rapamycin activation determined by Akt
    • Dan, H. C., and Baldwin, A. S. (2008) Differential involvement of IKKα and -β in cytokine- and insulin-induced mammalian target of rapamycin activation determined by Akt. J. Immunol. 180, 7582-7589
    • (2008) J. Immunol. , vol.180 , pp. 7582-7589
    • Dan, H.C.1    Baldwin, A.S.2
  • 40
    • 0037178786 scopus 로고    scopus 로고
    • mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim, D. H., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument-Bromage, H., Tempst, P., and Sabatini, D. M. (2002) mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163-175
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 41
    • 79960349522 scopus 로고    scopus 로고
    • mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth, and cell cycle progression
    • Ekim, B., Magnuson, B., Acosta-Jaquez, H. A., Keller, J. A., Feener, E. P., and Fingar, D. C. (2011) mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth, and cell cycle progression. Mol. Cell. Biol. 31, 2787-2801
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2787-2801
    • Ekim, B.1    Magnuson, B.2    Acosta-Jaquez, H.A.3    Keller, J.A.4    Feener, E.P.5    Fingar, D.C.6
  • 44
    • 0033961280 scopus 로고    scopus 로고
    • Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB
    • Madrid, L. V., Wang, C. Y., Guttridge, D. C., Schottelius, A. J., Baldwin, A. S., Jr., and Mayo, M. W. (2000) Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB. Mol. Cell. Biol. 20, 1626-1638
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1626-1638
    • Madrid, L.V.1    Wang, C.Y.2    Guttridge, D.C.3    Schottelius, A.J.4    Baldwin, A.S.5    Mayo, M.W.6
  • 45
    • 33745199637 scopus 로고    scopus 로고
    • Akt regulates basal and induced processing of NF-κB2 (p100) to p52
    • Gustin, J. A., Korgaonkar, C. K., Pincheira, R., Li, Q., and Donner, D. B. (2006) Akt regulates basal and induced processing of NF-κB2 (p100) to p52. J. Biol. Chem. 281, 16473-16481
    • (2006) J. Biol. Chem. , vol.281 , pp. 16473-16481
    • Gustin, J.A.1    Korgaonkar, C.K.2    Pincheira, R.3    Li, Q.4    Donner, D.B.5
  • 46
    • 0033517189 scopus 로고    scopus 로고
    • NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes, O. N., Mayo, L. D., Gustin, J. A., Pfeffer, S. R., Pfeffer, L. M., Donner, D. B. (1999) NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 401, 82-85
    • (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
  • 48
    • 79953773106 scopus 로고    scopus 로고
    • IKK-dependent, NF-κB-independent control of autophagic gene expression
    • Comb, W. C., Cogswell, P., Sitcheran, R., and Baldwin A. S. (2011) IKK-dependent, NF-κB-independent control of autophagic gene expression. Oncogene 30, 1727-1732
    • (2011) Oncogene , vol.30 , pp. 1727-1732
    • Comb, W.C.1    Cogswell, P.2    Sitcheran, R.3    Baldwin, A.S.4
  • 49
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco I., and Sawyers, C. L. (2002) The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat. Rev. Cancer 2, 489-501
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 50
    • 24944480788 scopus 로고    scopus 로고
    • The Akt-mTOR tango and its relevance to cancer
    • Hay, N. (2005) The Akt-mTOR tango and its relevance to cancer. Cancer Cell 8, 179-183
    • (2005) Cancer Cell , vol.8 , pp. 179-183
    • Hay, N.1
  • 52
    • 27844526600 scopus 로고    scopus 로고
    • Akt-dependent transformation: There is more to growth than just surviving
    • Plas, D. R., and Thompson, C. B. (2005) Akt-dependent transformation: there is more to growth than just surviving. Oncogene 24, 7435-7442
    • (2005) Oncogene , vol.24 , pp. 7435-7442
    • Plas, D.R.1    Thompson, C.B.2
  • 57
    • 23744484194 scopus 로고    scopus 로고
    • Genetic analysis of Pten and Tsc2 functional interactions in the mouse reveals asymmetrical haploinsufficiency in tumor suppression
    • Ma, L., Teruya-Feldstein, J., Behrendt, N., Chen, Z., Noda, T., Hino, O., Cordon-Cardo, C., and Pandolfi, P. P. (2005) Genetic analysis of Pten and Tsc2 functional interactions in the mouse reveals asymmetrical haploinsufficiency in tumor suppression. Genes Dev. 19, 1779-1786
    • (2005) Genes Dev. , vol.19 , pp. 1779-1786
    • Ma, L.1    Teruya-Feldstein, J.2    Behrendt, N.3    Chen, Z.4    Noda, T.5    Hino, O.6    Cordon-Cardo, C.7    Pandolfi, P.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.