메뉴 건너뛰기




Volumn 29, Issue 5, 2008, Pages 541-551

Loss of the Tuberous Sclerosis Complex Tumor Suppressors Triggers the Unfolded Protein Response to Regulate Insulin Signaling and Apoptosis

Author keywords

CELLCYCLE; PROTEINS; SIGNALING

Indexed keywords

CHAPERONE; INSULIN; INSULIN RECEPTOR; MAMMALIAN TARGET OF RAPAMYCIN; TUBERIN;

EID: 40649104735     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.12.023     Document Type: Article
Times cited : (381)

References (51)
  • 1
    • 0034708832 scopus 로고    scopus 로고
    • The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307)
    • Aguirre V., Uchida T., Yenush L., Davis R., and White M.F. The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). J. Biol. Chem. 275 (2000) 9047-9054
    • (2000) J. Biol. Chem. , vol.275 , pp. 9047-9054
    • Aguirre, V.1    Uchida, T.2    Yenush, L.3    Davis, R.4    White, M.F.5
  • 3
    • 33645154135 scopus 로고    scopus 로고
    • Cellular response to endoplasmic reticulum stress: a matter of life or death
    • Boyce M., and Yuan J. Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ. 13 (2006) 363-373
    • (2006) Cell Death Differ. , vol.13 , pp. 363-373
    • Boyce, M.1    Yuan, J.2
  • 4
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M., Zeng H., Urano F., Till J.H., Hubbard S.R., Harding H.P., Clark S.G., and Ron D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415 (2002) 92-96
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 5
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox J.S., Shamu C.E., and Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73 (1993) 1197-1206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 6
    • 33646548305 scopus 로고    scopus 로고
    • The amino acid sensitive TOR pathway from yeast to mammals
    • Dann S.G., and Thomas G. The amino acid sensitive TOR pathway from yeast to mammals. FEBS Lett. 580 (2006) 2821-2829
    • (2006) FEBS Lett. , vol.580 , pp. 2821-2829
    • Dann, S.G.1    Thomas, G.2
  • 9
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P., Zhang Y., and Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397 (1999) 271-274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 10
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding H.P., Zhang Y., Bertolotti A., Zeng H., and Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5 (2000) 897-904
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 13
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N., and Sonenberg N. Upstream and downstream of mTOR. Genes Dev. 18 (2004) 1926-1945
    • (2004) Genes Dev. , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 15
    • 33644750396 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress and c-Jun NH2-terminal kinase pathways in inflammation and origin of obesity and diabetes
    • Hotamisligil G.S. Role of endoplasmic reticulum stress and c-Jun NH2-terminal kinase pathways in inflammation and origin of obesity and diabetes. Diabetes 54 (2005) S73-S78
    • (2005) Diabetes , vol.54
    • Hotamisligil, G.S.1
  • 16
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • Hotamisligil G.S. Inflammation and metabolic disorders. Nature 444 (2006) 860-867
    • (2006) Nature , vol.444 , pp. 860-867
    • Hotamisligil, G.S.1
  • 17
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance
    • Hotamisligil G.S., Peraldi P., Budavari A., Ellis R., White M.F., and Spiegelman B.M. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance. Science 271 (1996) 665-668
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 18
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki K., Li Y., Zhu T., Wu J., and Guan K.L. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 4 (2002) 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
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki K., Zhu T., and Guan K.L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115 (2003) 577-590
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 20
    • 11244297916 scopus 로고    scopus 로고
    • Dysregulation of the TSC-mTOR pathway in human disease
    • Inoki K., Corradetti M.N., and Guan K.L. Dysregulation of the TSC-mTOR pathway in human disease. Nat. Genet. 37 (2005) 19-24
    • (2005) Nat. Genet. , vol.37 , pp. 19-24
    • Inoki, K.1    Corradetti, M.N.2    Guan, K.L.3
  • 21
    • 14244256097 scopus 로고    scopus 로고
    • Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance
    • Khamzina L., Veilleux A., Bergeron S., and Marette A. Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance. Endocrinology 146 (2005) 1473-1481
    • (2005) Endocrinology , vol.146 , pp. 1473-1481
    • Khamzina, L.1    Veilleux, A.2    Bergeron, S.3    Marette, A.4
  • 23
    • 0037623417 scopus 로고    scopus 로고
    • GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • Kim D.H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V., Erdjument-Bromage H., Tempst P., and Sabatini D.M. GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol. Cell 11 (2003) 895-904
    • (2003) Mol. Cell , vol.11 , pp. 895-904
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    Latek, R.R.4    Guntur, K.V.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 24
    • 0033559663 scopus 로고    scopus 로고
    • Renal carcinogenesis, hepatic hemangiomatosis, and embryonic lethality caused by a germ-line Tsc2 mutation in mice
    • Kobayashi T., Minowa O., Kuno J., Mitani H., Hino O., and Noda T. Renal carcinogenesis, hepatic hemangiomatosis, and embryonic lethality caused by a germ-line Tsc2 mutation in mice. Cancer Res. 59 (1999) 1206-1211
    • (1999) Cancer Res. , vol.59 , pp. 1206-1211
    • Kobayashi, T.1    Minowa, O.2    Kuno, J.3    Mitani, H.4    Hino, O.5    Noda, T.6
  • 25
    • 27744588780 scopus 로고    scopus 로고
    • Tuberous sclerosis: a GAP at the crossroads of multiple signaling pathways
    • Kwiatkowski D.J., and Manning B.D. Tuberous sclerosis: a GAP at the crossroads of multiple signaling pathways. Hum. Mol. Genet. 14 Spec No. 2 (2005) R251-R258
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.Spec 2
    • Kwiatkowski, D.J.1    Manning, B.D.2
  • 26
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee A.H., Iwakoshi N.N., and Glimcher L.H. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23 (2003) 7448-7459
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 29
    • 17444431201 scopus 로고    scopus 로고
    • Phosphorylation and functional inactivation of TSC2 by Erk: implications for tuberous sclerosis and cancer pathogenesis
    • Ma L., Chen Z., Erdjument-Bromage H., Tempst P., and Pandolfi P.P. Phosphorylation and functional inactivation of TSC2 by Erk: implications for tuberous sclerosis and cancer pathogenesis. Cell 121 (2005) 179-193
    • (2005) Cell , vol.121 , pp. 179-193
    • Ma, L.1    Chen, Z.2    Erdjument-Bromage, H.3    Tempst, P.4    Pandolfi, P.P.5
  • 30
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • Manning B.D., Tee A.R., Logsdon M.N., Blenis J., and Cantley L.C. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol. Cell 10 (2002) 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
  • 32
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak S.J., and Ron D. Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86 (2006) 1133-1149
    • (2006) Physiol. Rev. , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 33
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28- related kinase activity is required for signaling from the ER to the nucleus
    • Mori K., Ma W., Gething M.J., and Sambrook J. A transmembrane protein with a cdc2+/CDC28- related kinase activity is required for signaling from the ER to the nucleus. Cell 74 (1993) 743-756
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 34
    • 0032741978 scopus 로고    scopus 로고
    • Tsc2(+/-) mice develop tumors in multiple sites that express gelsolin and are influenced by genetic background
    • Onda H., Lueck A., Marks P.W., Warren H.B., and Kwiatkowski D.J. Tsc2(+/-) mice develop tumors in multiple sites that express gelsolin and are influenced by genetic background. J. Clin. Invest. 104 (1999) 687-695
    • (1999) J. Clin. Invest. , vol.104 , pp. 687-695
    • Onda, H.1    Lueck, A.2    Marks, P.W.3    Warren, H.B.4    Kwiatkowski, D.J.5
  • 37
    • 4544384577 scopus 로고    scopus 로고
    • Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
    • Roux P.P., Ballif B.A., Anjum R., Gygi S.P., and Blenis J. Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc. Natl. Acad. Sci. USA 101 (2004) 13489-13494
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13489-13494
    • Roux, P.P.1    Ballif, B.A.2    Anjum, R.3    Gygi, S.P.4    Blenis, J.5
  • 39
    • 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. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307 (2005) 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
  • 40
    • 0038643484 scopus 로고    scopus 로고
    • Rheb promotes cell growth as a component of the insulin/TOR signalling network
    • Saucedo L.J., Gao X., Chiarelli D.A., Li L., Pan D., and Edgar B.A. Rheb promotes cell growth as a component of the insulin/TOR signalling network. Nat. Cell Biol. 5 (2003) 566-571
    • (2003) Nat. Cell Biol. , vol.5 , pp. 566-571
    • Saucedo, L.J.1    Gao, X.2    Chiarelli, D.A.3    Li, L.4    Pan, D.5    Edgar, B.A.6
  • 41
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M., and Kaufman R.J. The mammalian unfolded protein response. Annu. Rev. Biochem. 74 (2005) 739-789
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 42
    • 4544343980 scopus 로고    scopus 로고
    • Inappropriate activation of the TSC/Rheb/mTOR/S6K cassette induces IRS1/2 depletion, insulin resistance, and cell survival deficiencies
    • Shah O.J., Wang Z., and Hunter T. Inappropriate activation of the TSC/Rheb/mTOR/S6K cassette induces IRS1/2 depletion, insulin resistance, and cell survival deficiencies. Curr. Biol. 14 (2004) 1650-1656
    • (2004) Curr. Biol. , vol.14 , pp. 1650-1656
    • Shah, O.J.1    Wang, Z.2    Hunter, T.3
  • 43
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee A.R., Manning B.D., Roux P.P., Cantley L.C., and Blenis J. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr. Biol. 13 (2003) 1259-1268
    • (2003) Curr. Biol. , vol.13 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 45
    • 33644886769 scopus 로고    scopus 로고
    • Nutrients suppress phosphatidylinositol 3-kinase/Akt via paptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation
    • Tzatsos A., and Kandror K.V. Nutrients suppress phosphatidylinositol 3-kinase/Akt via paptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation. Mol. Cell. Biol. 26 (2006) 63-76
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 63-76
    • Tzatsos, A.1    Kandror, K.V.2
  • 47
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F., Wang X., Bertolotti A., Zhang Y., Chung P., Harding H.P., and Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287 (2000) 664-666
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 48
    • 33847652935 scopus 로고    scopus 로고
    • Neocortical hyperexcitability in a human case of tuberous sclerosis complex and mice lacking neuronal expression of TSC1
    • Wang Y., Greenwood J.S., Calcagnotto M.E., Kirsch H.E., Barbaro N.M., and Baraban S.C. Neocortical hyperexcitability in a human case of tuberous sclerosis complex and mice lacking neuronal expression of TSC1. Ann. Neurol. 61 (2007) 139-152
    • (2007) Ann. Neurol. , vol.61 , pp. 139-152
    • Wang, Y.1    Greenwood, J.S.2    Calcagnotto, M.E.3    Kirsch, H.E.4    Barbaro, N.M.5    Baraban, S.C.6
  • 49
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., and Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107 (2001) 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 50
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • Zhang Y., Gao X., Saucedo L.J., Ru B., Edgar B.A., and Pan D. Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nat. Cell Biol. 5 (2003) 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
  • 51
    • 33244481462 scopus 로고    scopus 로고
    • Ser/Thr phosphorylation of IRS proteins: a molecular basis for insulin resistance
    • Zick Y. Ser/Thr phosphorylation of IRS proteins: a molecular basis for insulin resistance. Sci. STKE 2005 (2005) pe4
    • (2005) Sci. STKE , vol.2005
    • Zick, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.