메뉴 건너뛰기




Volumn 14, Issue 8, 2015, Pages 2042-2055

Functional proteomics identifies acinus L as a direct insulin- and amino acid-dependent mammalian target of rapamycin complex 1 (mTORC1) substrate

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; INSULIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; PROTEIN ACINUS L; PROTEINASE; UNCLASSIFIED DRUG; ACIN1 PROTEIN, HUMAN; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; NUCLEAR PROTEIN; PHOSPHOPROTEIN; PROTEOME; RPTOR PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TARGET OF RAPAMYCIN KINASE;

EID: 84938918891     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.045807     Document Type: Article
Times cited : (15)

References (91)
  • 2
    • 84859778293 scopus 로고    scopus 로고
    • mTOR signaling in growth control and disease
    • Laplante, M., and Sabatini, D. M. (2012) mTOR signaling in growth control and disease. Cell 149, 274-293
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.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
    • 84881479778 scopus 로고    scopus 로고
    • Targeting the PI3K/AKT/mTOR signaling pathway in glioblastoma: Novel therapeutic agents and advances in understanding
    • Sami, A., and Karsy, M. (2013) Targeting the PI3K/AKT/mTOR signaling pathway in glioblastoma: novel therapeutic agents and advances in understanding. Tumour Biol. 34, 1991-2002
    • (2013) Tumour Biol. , vol.34 , pp. 1991-2002
    • Sami, A.1    Karsy, M.2
  • 5
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Ruegg, M. A., Hall, A., and Hall, M. N. (2004) Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat.Cell Biol. 6, 1122-1128
    • (2004) Nat.Cell Biol. , vol.6 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3    Lin, S.4    Ruegg, M.A.5    Hall, A.6    Hall, M.N.7
  • 7
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • Sarbassov, D. D., Ali, S. M., Kim, D. H., Guertin, D. A., Latek, R. R., Erdjument-Bromage, H., Tempst, P., and Sabatini, D. M. (2004) Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr. Biol. 14, 1296-1302
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 8
    • 67349241955 scopus 로고    scopus 로고
    • DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival
    • Peterson, T. R., Laplante, M., Thoreen, C. C., Sancak, Y., Kang, S. A., Kuehl, W. M., Gray, N. S., and Sabatini, D. M. (2009) DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell 137, 873-886
    • (2009) Cell , vol.137 , pp. 873-886
    • Peterson, T.R.1    Laplante, M.2    Thoreen, C.C.3    Sancak, Y.4    Kang, S.A.5    Kuehl, W.M.6    Gray, N.S.7    Sabatini, D.M.8
  • 9
    • 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
  • 11
    • 33749076673 scopus 로고    scopus 로고
    • SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity
    • Jacinto, E., Facchinetti, V., Liu, D., Soto, N., Wei, S., Jung, S. Y., Huang, Q., Qin, J., and Su, B. (2006) SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell 127, 125-137
    • (2006) Cell , vol.127 , pp. 125-137
    • Jacinto, E.1    Facchinetti, V.2    Liu, D.3    Soto, N.4    Wei, S.5    Jung, S.Y.6    Huang, Q.7    Qin, J.8    Su, B.9
  • 12
    • 33748471980 scopus 로고    scopus 로고
    • mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s
    • Frias, M. A., Thoreen, C. C., Jaffe, J. D., Schroder, W., Sculley, T., Carr, S. A., and Sabatini, D. M. (2006) mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s. Curr. Biol. 16, 1865-1870
    • (2006) Curr. Biol. , vol.16 , pp. 1865-1870
    • Frias, M.A.1    Thoreen, C.C.2    Jaffe, J.D.3    Schroder, W.4    Sculley, T.5    Carr, S.A.6    Sabatini, D.M.7
  • 13
    • 33751079895 scopus 로고    scopus 로고
    • Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity
    • Yang, Q., Inoki, K., Ikenoue, T., and Guan, K. L. (2006) Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity. Genes Dev. 20, 2820-2832
    • (2006) Genes Dev. , vol.20 , pp. 2820-2832
    • Yang, Q.1    Inoki, K.2    Ikenoue, T.3    Guan, K.L.4
  • 16
    • 34548509880 scopus 로고    scopus 로고
    • PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling
    • Woo, S. Y., Kim, D. H., Jun, C. B., Kim, Y. M., Haar, E. V., Lee, S. I., Hegg, J. W., Bandhakavi, S., Griffin, T. J., and Kim, D. H. (2007) PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling. J. Biol. Chem. 282, 25604-25612
    • (2007) J. Biol. Chem. , vol.282 , pp. 25604-25612
    • Woo, S.Y.1    Kim, D.H.2    Jun, C.B.3    Kim, Y.M.4    Haar, E.V.5    Lee, S.I.6    Hegg, J.W.7    Bandhakavi, S.8    Griffin, T.J.9    Kim, D.H.10
  • 19
    • 80155142474 scopus 로고    scopus 로고
    • Rapamycin passes the torch: A new generation of mTOR inhibitors
    • Benjamin, D., Colombi, M., Moroni, C., and Hall, M. N. (2011) Rapamycin passes the torch: a new generation of mTOR inhibitors. Nat. Rev. Drug Discov. 10, 868-880
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 868-880
    • Benjamin, D.1    Colombi, M.2    Moroni, C.3    Hall, M.N.4
  • 21
    • 84878532557 scopus 로고    scopus 로고
    • Signal integration by mTORC1 coordinates nutrient input with biosynthetic output
    • Dibble, C. C., and Manning, B. D. (2013) Signal integration by mTORC1 coordinates nutrient input with biosynthetic output. Nat. Cell Biol. 15, 555-564
    • (2013) Nat. Cell Biol. , vol.15 , pp. 555-564
    • Dibble, C.C.1    Manning, B.D.2
  • 22
    • 78650510609 scopus 로고    scopus 로고
    • mTOR: From growth signal integration to cancer, diabetes, and aging
    • Zoncu, R., Efeyan, A., and Sabatini, D. M. (2011) mTOR: from growth signal integration to cancer, diabetes, and aging. 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
  • 23
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha
    • Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R., Reese, C. B., and Cohen, P. (1997) Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. Curr. Biol. 7, 261-269
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6    Cohen, P.7
  • 24
    • 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
  • 25
    • 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. (2002) 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, 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
  • 28
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki, K., Li, Y., Xu, T., and Guan, K. L. (2003) Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 17, 1829-1834
    • (2003) Genes Dev. , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 29
    • 0038643484 scopus 로고    scopus 로고
    • Rheb promotes cell growth as a component of the insulin/TOR signaling network
    • Saucedo, L. J., Gao, X., Chiarelli, D. A., Li, L., Pan, D., and Edgar, B. A. (2003) Rheb promotes cell growth as a component of the insulin/TOR signaling network. Nat. Cell Biol. 5, 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
  • 30
    • 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. (2003) Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr. Biol. 13, 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
  • 31
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., and Sabatini, D. M. (2010) Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141, 290-303
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 32
    • 59749087582 scopus 로고    scopus 로고
    • Rag proteins regulate amino-acid-induced mTORC1 signaling
    • Sancak, Y., and Sabatini, D. M. (2009) Rag proteins regulate amino-acid-induced mTORC1 signaling. Biochem. Soc. Trans. 37, 289-290
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 289-290
    • Sancak, Y.1    Sabatini, D.M.2
  • 33
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., Zhu, T., and Guan, K. L. (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 39
    • 34548359244 scopus 로고    scopus 로고
    • PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex
    • Fonseca, B. D., Smith, E. M., Lee, V. H., MacKintosh, C., and Proud, C. G. (2007) PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex. J. Biol. Chem. 282, 24514-24524
    • (2007) J. Biol. Chem. , vol.282 , pp. 24514-24524
    • Fonseca, B.D.1    Smith, E.M.2    Lee, V.H.3    MacKintosh, C.4    Proud, C.G.5
  • 41
    • 47049127002 scopus 로고    scopus 로고
    • Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation
    • Wang, L., Harris, T. E., and Lawrence, J. C., Jr. (2008) Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation. J. Biol. Chem. 283, 15619-15627
    • (2008) J. Biol. Chem. , vol.283 , pp. 15619-15627
    • Wang, L.1    Harris, T.E.2    Lawrence, J.C.3
  • 42
    • 34247118887 scopus 로고    scopus 로고
    • Signaling to translation: How signal transduction pathways control the protein synthetic machinery
    • Proud, C. G. (2007) Signaling to translation: how signal transduction pathways control the protein synthetic machinery. Biochem. J. 403, 217-234
    • (2007) Biochem. J. , vol.403 , pp. 217-234
    • Proud, C.G.1
  • 43
    • 84882884638 scopus 로고    scopus 로고
    • Translational Control by Amino Acids and Energy
    • Dennis, R. B. a. E., ed.
    • Thedieck, K., and Hall, M. N. (2009) Translational Control by Amino Acids and Energy. In: Dennis, R. B. a. E., ed. The Handbook of Cell Signaling, 2 Ed., pp. 2285-2293
    • (2009) The Handbook of Cell Signaling, 2 Ed. , pp. 2285-2293
    • Thedieck, K.1    Hall, M.N.2
  • 46
    • 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
  • 47
    • 84874995247 scopus 로고    scopus 로고
    • Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1
    • Ben-Sahra, I., Howell, J. J., Asara, J. M., and Manning, B. D. (2013) Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1. Science 339, 1323-1328
    • (2013) Science , vol.339 , pp. 1323-1328
    • Ben-Sahra, I.1    Howell, J.J.2    Asara, J.M.3    Manning, B.D.4
  • 51
    • 79953211540 scopus 로고    scopus 로고
    • Amino acids activate mammalian target of rapamycin complex 2 (mTORC2) via PI3K/ Akt signaling
    • Tato, I., Bartrons, R., Ventura, F., and Rosa, J. L. (2011) Amino acids activate mammalian target of rapamycin complex 2 (mTORC2) via PI3K/ Akt signaling. J. Biol. Chem. 286, 6128-6142
    • (2011) J. Biol. Chem. , vol.286 , pp. 6128-6142
    • Tato, I.1    Bartrons, R.2    Ventura, F.3    Rosa, J.L.4
  • 52
    • 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
  • 53
    • 28844434558 scopus 로고    scopus 로고
    • mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes
    • Hresko, R. C., and Mueckler, M. (2005) mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes. J. Biol. Chem. 280, 40406-40416
    • (2005) J. Biol. Chem. , vol.280 , pp. 40406-40416
    • Hresko, R.C.1    Mueckler, M.2
  • 54
    • 58649092475 scopus 로고    scopus 로고
    • mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)
    • Garcia-Martinez, J. M., and Alessi, D. R. (2008) mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1). Biochem. J. 416, 375-385
    • (2008) Biochem. J. , vol.416 , pp. 375-385
    • Garcia-Martinez, J.M.1    Alessi, D.R.2
  • 55
    • 47949104258 scopus 로고    scopus 로고
    • Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation, and signaling
    • Ikenoue, T., Inoki, K., Yang, Q., Zhou, X., and Guan, K. L. (2008) Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation, and signaling. EMBO J. 27, 1919-1931
    • (2008) EMBO J. , vol.27 , pp. 1919-1931
    • Ikenoue, T.1    Inoki, K.2    Yang, Q.3    Zhou, X.4    Guan, K.L.5
  • 58
    • 39749100492 scopus 로고    scopus 로고
    • TOR regulation of AGC kinases in yeast and mammals
    • Jacinto, E., and Lorberg, A. (2008) TOR regulation of AGC kinases in yeast and mammals. Biochem. J. 410, 19-37
    • (2008) Biochem. J. , vol.410 , pp. 19-37
    • Jacinto, E.1    Lorberg, A.2
  • 60
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 61
    • 85027920901 scopus 로고    scopus 로고
    • A modeling-experimental approach reveals insulin receptor substrate (IRS)-dependent regulation of adenosine monosphosphate-dependent kinase (AMPK) by insulin
    • Sonntag, A. G., Dalle Pezze, P., Shanley, D. P., and Thedieck, K. (2012) A modeling-experimental approach reveals insulin receptor substrate (IRS)-dependent regulation of adenosine monosphosphate-dependent kinase (AMPK) by insulin. FEBS J. 279, 3314-3328
    • (2012) FEBS J. , vol.279 , pp. 3314-3328
    • Sonntag, A.G.1    Dalle Pezze, P.2    Shanley, D.P.3    Thedieck, K.4
  • 63
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara, S., Aoto, M., Eguchi, Y., Imamoto, N., Yoneda, Y., and Tsujimoto, Y. (1999) Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature 401, 168-173
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 64
    • 79961217471 scopus 로고    scopus 로고
    • Comparison of ERLIC-TiO2, HILIC-TiO2, and SCX-TiO2 for global phosphoproteomics approaches
    • Zarei, M., Sprenger, A., Metzger, F., Gretzmeier, C., and Dengjel, J. (2011) Comparison of ERLIC-TiO2, HILIC-TiO2, and SCX-TiO2 for global phosphoproteomics approaches. J. Proteome Res. 10, 3474-3483
    • (2011) J. Proteome Res. , vol.10 , pp. 3474-3483
    • Zarei, M.1    Sprenger, A.2    Metzger, F.3    Gretzmeier, C.4    Dengjel, J.5
  • 66
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 72
    • 0025837327 scopus 로고
    • Mitogen-activated 70K S6 kinase. Identification of in vitro 40 S ribosomal S6 phosphorylation sites
    • Ferrari, S., Bandi, H. R., Hofsteenge, J., Bussian, B. M., and Thomas, G. (1991) Mitogen-activated 70K S6 kinase. Identification of in vitro 40 S ribosomal S6 phosphorylation sites. J. Biol. Chem. 266, 22770-22775
    • (1991) J. Biol. Chem. , vol.266 , pp. 22770-22775
    • Ferrari, S.1    Bandi, H.R.2    Hofsteenge, J.3    Bussian, B.M.4    Thomas, G.5
  • 73
    • 0026659046 scopus 로고
    • Rapamycin- FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases
    • Chung, J., Kuo, C. J., Crabtree, G. R., and Blenis, J. (1992) Rapamycin- FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases. Cell 69, 1227-1236
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3    Blenis, J.4
  • 74
    • 34347242470 scopus 로고    scopus 로고
    • RAS/ERK signaling promotes sitespecific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation
    • Roux, P. P., Shahbazian, D., Vu, H., Holz, M. K., Cohen, M. S., Taunton, J., Sonenberg, N., and Blenis, J. (2007) RAS/ERK signaling promotes sitespecific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation. J. Biol. Chem. 282, 14056-14064
    • (2007) J. Biol. Chem. , vol.282 , pp. 14056-14064
    • Roux, P.P.1    Shahbazian, D.2    Vu, H.3    Holz, M.K.4    Cohen, M.S.5    Taunton, J.6    Sonenberg, N.7    Blenis, J.8
  • 75
    • 67649344456 scopus 로고    scopus 로고
    • Mammalian target of rapamycin complex 1 (mTORC1) activity is associated with phosphorylation of raptor by mTOR
    • Wang, L., Lawrence, J. C., Jr., Sturgill, T. W., and Harris, T. E. (2009) Mammalian target of rapamycin complex 1 (mTORC1) activity is associated with phosphorylation of raptor by mTOR. J. Biol. Chem. 284, 14693-14697
    • (2009) J. Biol. Chem. , vol.284 , pp. 14693-14697
    • Wang, L.1    Lawrence, J.C.2    Sturgill, T.W.3    Harris, T.E.4
  • 77
    • 0034141942 scopus 로고    scopus 로고
    • Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI
    • Raught, B., Gingras, A. C., Gygi, S. P., Imataka, H., Morino, S., Gradi, A., Aebersold, R., and Sonenberg, N. (2000) Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI. EMBO J. 19, 434-444
    • (2000) EMBO J. , vol.19 , pp. 434-444
    • Raught, B.1    Gingras, A.C.2    Gygi, S.P.3    Imataka, H.4    Morino, S.5    Gradi, A.6    Aebersold, R.7    Sonenberg, N.8
  • 78
    • 42449138319 scopus 로고    scopus 로고
    • eIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy
    • Ramirez-Valle, F., Braunstein, S., Zavadil, J., Formenti, S. C., and Schneider, R. J. (2008) eIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy. J. Cell Biol. 181, 293-307
    • (2008) J. Cell Biol. , vol.181 , pp. 293-307
    • Ramirez-Valle, F.1    Braunstein, S.2    Zavadil, J.3    Formenti, S.C.4    Schneider, R.J.5
  • 79
    • 0028036698 scopus 로고
    • Insulin receptor substrate-1 mediates phosphatidylinositol 3′-kinase and p70S6k signaling during insulin, insulin-like growth factor-1, and interleukin-4 stimulation
    • Myers, M. G., Jr., Grammer, T. C., Wang, L. M., Sun, X. J., Pierce, J. H., Blenis, J., and White, M. F. (1994) Insulin receptor substrate-1 mediates phosphatidylinositol 3′-kinase and p70S6k signaling during insulin, insulin-like growth factor-1, and interleukin-4 stimulation. J. Biol. Chem. 269, 28783-28789
    • (1994) J. Biol. Chem. , vol.269 , pp. 28783-28789
    • Myers, M.G.1    Grammer, T.C.2    Wang, L.M.3    Sun, X.J.4    Pierce, J.H.5    Blenis, J.6    White, M.F.7
  • 80
    • 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. (2004) Inappropriate activation of the TSC/Rheb/mTOR/S6K cassette induces IRS1/2 depletion, insulin resistance, and cell survival deficiencies. Curr. Biol. 14, 1650-1656
    • (2004) Curr. Biol. , vol.14 , pp. 1650-1656
    • Shah, O.J.1    Wang, Z.2    Hunter, T.3
  • 84
    • 41949101770 scopus 로고    scopus 로고
    • SKAR links premRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs
    • Ma, X. M., Yoon, S. O., Richardson, C. J., Julich, K., and Blenis, J. (2008) SKAR links premRNA splicing to mTOR/S6K1-mediated enhanced translation efficiency of spliced mRNAs. Cell 133, 303-313
    • (2008) Cell , vol.133 , pp. 303-313
    • Ma, X.M.1    Yoon, S.O.2    Richardson, C.J.3    Julich, K.4    Blenis, J.5
  • 85
    • 0942268832 scopus 로고    scopus 로고
    • Splicing enhances translation in mammalian cells: An additional function of the exon junction complex
    • Nott, A., Le Hir, H., and Moore, M. J. (2004) Splicing enhances translation in mammalian cells: an additional function of the exon junction complex. Genes Dev. 18, 210-222
    • (2004) Genes Dev. , vol.18 , pp. 210-222
    • Nott, A.1    Le Hir, H.2    Moore, M.J.3
  • 86
    • 0035823247 scopus 로고    scopus 로고
    • Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1
    • Lykke-Andersen, J., Shu, M. D., and Steitz, J. A. (2001) Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science 293, 1836-1839
    • (2001) Science , vol.293 , pp. 1836-1839
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 87
    • 49649101933 scopus 로고    scopus 로고
    • Serine/arginine protein-specific kinase 2 promotes leukemia cell proliferation by phosphorylating acinus and regulating cyclin A1
    • Jang, S. W., Yang, S. J., Ehlen, A., Dong, S., Khoury, H., Chen, J., Persson, J. L., and Ye, K. (2008) Serine/arginine protein-specific kinase 2 promotes leukemia cell proliferation by phosphorylating acinus and regulating cyclin A1. Cancer Res. 68, 4559-4570
    • (2008) Cancer Res. , vol.68 , pp. 4559-4570
    • Jang, S.W.1    Yang, S.J.2    Ehlen, A.3    Dong, S.4    Khoury, H.5    Chen, J.6    Persson, J.L.7    Ye, K.8
  • 88
    • 2342540912 scopus 로고    scopus 로고
    • The ever-increasing complexities of the exon junction complex
    • Tange, T. O., Nott, A., and Moore, M. J. (2004) The ever-increasing complexities of the exon junction complex. Curr. Opin. Cell Biol. 16, 279-284
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 279-284
    • Tange, T.O.1    Nott, A.2    Moore, M.J.3
  • 89
    • 27144446343 scopus 로고    scopus 로고
    • Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation
    • Hu, Y., Yao, J., Liu, Z., Liu, X., Fu, H., and Ye, K. (2005) Akt phosphorylates acinus and inhibits its proteolytic cleavage, preventing chromatin condensation. EMBO J. 24, 3543-3554
    • (2005) EMBO J. , vol.24 , pp. 3543-3554
    • Hu, Y.1    Yao, J.2    Liu, Z.3    Liu, X.4    Fu, H.5    Ye, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.