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Volumn 183, Issue 11, 2009, Pages 7388-7397

MAPK, phosphatidylinositol 3-kinase, and mammalian target of rapamycin pathways converge at the level of ribosomal protein S6 phosphorylation to control metabolic signaling in CD8 T cells

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE FYN; PROTEIN KINASE LCK; PROTEIN S6; CARRIER PROTEIN; FRAP1 PROTEIN, MOUSE; FYN PROTEIN, MOUSE; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHOTRANSFERASE; S6 KINASE;

EID: 73349119966     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0902294     Document Type: Article
Times cited : (102)

References (49)
  • 1
    • 61449212998 scopus 로고    scopus 로고
    • T cell dependence on mTOR signaling
    • Mills, R. E., and J. M. Jameson. 2009. T cell dependence on mTOR signaling. Cell Cycle 8: 545-548.
    • (2009) Cell Cycle , vol.8 , pp. 545-548
    • Mills, R.E.1    Jameson, J.M.2
  • 2
    • 0037178781 scopus 로고    scopus 로고
    • Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action
    • DOI 10.1016/S0092-8674(02)00833-4
    • Hara, K., Y. Maruki, X. Long, K. Yoshino, N. Oshiro, S. Hidayat, C. Tokunaga, J. Avruch, and K. Yonezawa. 2002. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 110: 177-189. (Pubitemid 34876546)
    • (2002) Cell , vol.110 , Issue.2 , pp. 177-189
    • Hara, K.1    Maruki, Y.2    Long, X.3    Yoshino, K.-I.4    Oshiro, N.5    Hidayat, S.6    Tokunaga, C.7    Avruch, J.8    Yonezawa, K.9
  • 4
    • 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., S. M. Ali, D. H. Kim, D. A. Guertin, R. R. Latek, H. Erdjument-Bromage, P. Tempst, and D. M. Sabatini. 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
  • 6
    • 0025099697 scopus 로고
    • Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin
    • Dumont, F. J., M. J. Staruch, S. L. Koprak, M. R. Melino, and N. H. Sigal. 1990. Distinct mechanisms of suppression of murine T cell activation by the related macrolides FK-506 and rapamycin. J. Immunol. 144: 251-258.
    • (1990) J. Immunol. , vol.144 , pp. 251-258
    • Dumont, F.J.1    Staruch, M.J.2    Koprak, S.L.3    Melino, M.R.4    Sigal, N.H.5
  • 7
  • 9
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases
    • Chung, J., C. J. Kuo, G. R. Crabtree, and J. Blenis. 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
  • 11
    • 0030066934 scopus 로고    scopus 로고
    • Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation
    • Beretta, L., A. C. Gingras, Y. V. Svitkin, M. N. Hall, and N. Sonenberg. 1996. Rapamycin blocks the phosphorylation of 4E-BP1 and inhibits cap-dependent initiation of translation. EMBO J. 15: 658-664. (Pubitemid 26044579)
    • (1996) EMBO Journal , vol.15 , Issue.3 , pp. 658-664
    • Beretta, L.1    Gingras, A.-C.2    Svitkin, Y.V.3    Hall, M.N.4    Sonenberg, N.5
  • 13
    • 29144438951 scopus 로고    scopus 로고
    • Inactivation of S6 ribosomal protein gene in T lymphocytes activates a p53-dependent checkpoint response
    • DOI 10.1101/gad.359305
    • Sulic, S., L. Panic, M. Barkic, M. Mercep, M. Uzelac, and S. Volarevic. 2005. Inactivation of S6 ribosomal protein gene in T lymphocytes activates a p53-dependent checkpoint response. Genes Dev. 19: 3070-3082. (Pubitemid 41798121)
    • (2005) Genes and Development , vol.19 , Issue.24 , pp. 3070-3082
    • Sulic, S.1    Panic, L.2    Barkic, M.3    Mercep, M.4    Uzelac, M.5    Volarevic, S.6
  • 14
    • 0033761629 scopus 로고    scopus 로고
    • Synthesis of the translational apparatus is regulated at the translational level
    • Meyuhas, O. 2000. Synthesis of the translational apparatus is regulated at the translational level. Eur. J. Biochem. 267: 6321-6330.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6321-6330
    • Meyuhas, O.1
  • 16
    • 33750986199 scopus 로고    scopus 로고
    • Lck regulates the threshold of activation in primary T cells, while both Lck and Fyn contribute to the magnitude of the extracellular signal-related kinase response
    • DOI 10.1128/MCB.00168-06
    • Lovatt, M., A. Filby, V. Parravicini, G. Werlen, E. Palmer, and R. Zamoyska. 2006. Lck regulates the threshold of activation in primary T cells, while both Lck and Fyn contribute to the magnitude of the extracellular signal-related kinase response. Mol. Cell. Biol. 26: 8655-8665. (Pubitemid 44748595)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.22 , pp. 8655-8665
    • Lovatt, M.1    Filby, A.2    Parravicini, V.3    Werlen, G.4    Palmer, E.5    Zamoyska, R.6
  • 19
    • 61849090213 scopus 로고    scopus 로고
    • New insights into the regulation and function of serine/threonine kinases in T lymphocytes
    • Matthews, S. A., and D. A. Cantrell. 2009. New insights into the regulation and function of serine/threonine kinases in T lymphocytes. Immunol. Rev. 228: 241-252.
    • (2009) Immunol. Rev. , vol.228 , pp. 241-252
    • Matthews, S.A.1    Cantrell, D.A.2
  • 20
    • 61849128182 scopus 로고    scopus 로고
    • T-cell receptor proximal signaling via the Src-family kinases, Lck and Fyn, influences T-cell activation, differentiation, and tolerance
    • Salmond, R. J., A. Filby, I. Qureshi, S. Caserta, and R. Zamoyska. 2009. T-cell receptor proximal signaling via the Src-family kinases, Lck and Fyn, influences T-cell activation, differentiation, and tolerance. Immunol. Rev. 228: 9-22.
    • (2009) Immunol. Rev. , vol.228 , pp. 9-22
    • Salmond, R.J.1    Filby, A.2    Qureshi, I.3    Caserta, S.4    Zamoyska, R.5
  • 22
    • 0030740005 scopus 로고    scopus 로고
    • The modular phosphorylation and activation of p70s6k
    • Pullen, N., and G. Thomas. 1997. The modular phosphorylation and activation of p70s6k. FEBS Lett. 410: 78-82.
    • (1997) FEBS Lett. , vol.410 , pp. 78-82
    • Pullen, N.1    Thomas, G.2
  • 24
    • 0042847309 scopus 로고    scopus 로고
    • Mechanism of ribosomal p70S6 kinase activation by granulocyte macrophage colony-stimulating factor in neutrophils: Cooperation of a MEK-related, THR421/SER424 kinase and a rapamycin-sensitive, m-TOR-related THR389 kinase
    • Lehman, J. A., V. Calvo, and J. Gomez-Cambronero. 2003. Mechanism of ribosomal p70S6 kinase activation by granulocyte macrophage colony-stimulating factor in neutrophils: cooperation of a MEK-related, THR421/SER424 kinase and a rapamycin-sensitive, m-TOR-related THR389 kinase. J. Biol. Chem. 278: 28130-28138.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28130-28138
    • Lehman, J.A.1    Calvo, V.2    Gomez-Cambronero, J.3
  • 25
    • 38949150779 scopus 로고    scopus 로고
    • CD28 provides T-cell costimulation and enhances PI3K activity at the immune synapse independently of its capacity to interact with the p85/p110 heterodimer
    • DOI 10.1182/blood-2007-08-108050
    • Garcon, F., D. T. Patton, J. L. Emery, E. Hirsch, R. Rottapel, T. Sasaki, and K. Okkenhaug. 2008. CD28 provides T-cell costimulation and enhances PI3K activity at the immune synapse independently of its capacity to interact with the p85/p110 heterodimer. Blood 111: 1464-1471. (Pubitemid 351213434)
    • (2008) Blood , vol.111 , Issue.3 , pp. 1464-1471
    • Garcon, F.1    Patton, D.T.2    Emery, J.L.3    Hirsch, E.4    Rottapel, R.5    Sasaki, T.6    Okkenhaug, K.7
  • 26
    • 0033622135 scopus 로고    scopus 로고
    • lck in human peripheral blood T lymphocytes is dependent on costimulation through accessory receptors: Involvement of phospholipase C, protein kinase C and MAP-kinases in vivo
    • lck in human peripheral blood T lymphocytes is dependent on costimulation through accessory receptors: involvement of phospholipase C, protein kinase C and MAP-kinases in vivo. Eur. J. Immunol. 30: 635-643.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 635-643
    • Schroder, A.J.1    Quehl, P.2    Muller, J.3    Samstag, Y.4
  • 27
    • 30444439101 scopus 로고    scopus 로고
    • Key role of the p110δ isoform of PI3K in B-cell antigen and IL-4 receptor signaling: Comparative analysis of genetic and pharmacologic interference with p110δ function in B cells
    • DOI 10.1182/blood-2005-07-3041
    • Bilancio, A., K. Okkenhaug, M. Camps, J. L. Emery, T. Ruckle, C. Rommel, and B. Vanhaesebroeck. 2006. Key role of the p110δ isoform of PI3K in B-cell antigen and IL-4 receptor signaling: comparative analysis of genetic and pharmacologic interference with p110δ function in B cells. Blood 107: 642-650. (Pubitemid 43076389)
    • (2006) Blood , vol.107 , Issue.2 , pp. 642-650
    • Bilancio, A.1    Okkenhaug, K.2    Camps, M.3    Emery, J.L.4    Ruckle, T.5    Rommel, C.6    Vanhaesebroeck, B.7
  • 28
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002
    • Brunn, G. J., J. Williams, C. Sabers, G. Wiederrecht, J. C. Lawrence, Jr., and R. T. Abraham. 1996. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J. 15: 5256-5267.
    • (1996) EMBO J. , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Wiederrecht, G.4    Lawrence Jr., J.C.5    Abraham, R.T.6
  • 29
    • 45849105156 scopus 로고    scopus 로고
    • The rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • DOI 10.1126/science.1157535
    • Sancak, Y., T. R. Peterson, Y. D. Shaul, R. A. Lindquist, C. C. Thoreen, L. Bar-Peled, and D. M. Sabatini. 2008. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320: 1496-1501. (Pubitemid 351929429)
    • (2008) Science , vol.320 , Issue.5882 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3    Lindquist, R.A.4    Thoreen, C.C.5    Bar-Peled, L.6    Sabatini, D.M.7
  • 30
    • 33846621025 scopus 로고    scopus 로고
    • Antigen receptor signalling: A distinctive role for the p110δ isoform of PI3K
    • DOI 10.1016/j.it.2006.12.007, PII S147149060600353X
    • Okkenhaug, K., K. Ali, and B. Vanhaesebroeck. 2007. Antigen receptor signalling: a distinctive role for the p110δ isoform of PI3K. Trends Immunol. 28: 80-87. (Pubitemid 46176736)
    • (2007) Trends in Immunology , vol.28 , Issue.2 , pp. 80-87
    • Okkenhaug, K.1    Ali, K.2    Vanhaesebroeck, B.3
  • 32
    • 39749141485 scopus 로고    scopus 로고
    • The regulation and function of class III PI3Ks: Novel roles for Vps34
    • Backer, J. M. 2008. The regulation and function of class III PI3Ks: novel roles for Vps34. Biochem. J. 410: 1-17.
    • (2008) Biochem. J. , vol.410 , pp. 1-17
    • Backer, J.M.1
  • 34
    • 27744519400 scopus 로고    scopus 로고
    • Fuel feeds function: Energy metabolism and the T-cell response
    • Fox, C. J., P. S. Hammerman, and C. B. Thompson. 2005. Fuel feeds function: energy metabolism and the T-cell response. Nat. Rev. Immunol. 5: 844-852.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 844-852
    • Fox, C.J.1    Hammerman, P.S.2    Thompson, C.B.3
  • 35
    • 0036320205 scopus 로고    scopus 로고
    • Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake
    • Edinger, A. L., and C. B. Thompson. 2002. Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake. Mol. Biol. Cell 13: 2276-2288.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2276-2288
    • Edinger, A.L.1    Thompson, C.B.2
  • 39
  • 40
    • 26644459229 scopus 로고    scopus 로고
    • The role of erk1 and erk2 in multiple stages of T cell development
    • Fischer, A. M., C. D. Katayama, G. Pages, J. Pouyssegur, and S. M. Hedrick. 2005. The role of erk1 and erk2 in multiple stages of T cell development. Immunity 23: 431-443.
    • (2005) Immunity , vol.23 , pp. 431-443
    • Fischer, A.M.1    Katayama, C.D.2    Pages, G.3    Pouyssegur, J.4    Hedrick, S.M.5
  • 41
    • 38349096466 scopus 로고    scopus 로고
    • Critical role for Rsk2 in T-lymphocyte activation
    • Lin, J. X., R. Spolski, and W. J. Leonard. 2008. Critical role for Rsk2 in T-lymphocyte activation. Blood 111: 525-533.
    • (2008) Blood , vol.111 , pp. 525-533
    • Lin, J.X.1    Spolski, R.2    Leonard, W.J.3
  • 42
    • 34347242470 scopus 로고    scopus 로고
    • RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation
    • Roux, P. P., D. Shahbazian, H. Vu, M. K. Holz, M. S. Cohen, J. Taunton, N. Sonenberg, and J. Blenis. 2007. RAS/ERK signaling promotes site-specific 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
  • 43
    • 35348812273 scopus 로고    scopus 로고
    • Measuring phosphorylated Akt and other phosphoinositide 3-kinase-regulated phosphoproteins in primary lymphocytes
    • Donahue, A. C., M. G. Kharas, and D. A. Fruman. 2007. Measuring phosphorylated Akt and other phosphoinositide 3-kinase-regulated phosphoproteins in primary lymphocytes. Methods Enzymol. 434: 131-154.
    • (2007) Methods Enzymol. , vol.434 , pp. 131-154
    • Donahue, A.C.1    Kharas, M.G.2    Fruman, D.A.3
  • 44
    • 33847671760 scopus 로고    scopus 로고
    • Phosphorylation and functions of inhibitor-2 family of proteins
    • DOI 10.1021/bi602369m
    • Li, M., D. L. Satinover, and D. L. Brautigan. 2007. Phosphorylation and functions of inhibitor-2 family of proteins. Biochemistry 46: 2380-2389. (Pubitemid 46362412)
    • (2007) Biochemistry , vol.46 , Issue.9 , pp. 2380-2389
    • Li, M.1    Satinover, D.L.2    Brautigan, D.L.3
  • 46
    • 33847208485 scopus 로고    scopus 로고
    • PAG-associated FynT regulates calcium signaling and promotes anergy in T lymphocytes
    • DOI 10.1128/MCB.01983-06
    • Davidson, D., B. Schraven, and A. Veillette. 2007. PAG-associated FynT regulates calcium signaling and promotes anergy in T lymphocytes. Mol. Cell. Biol. 27: 1960-1973. (Pubitemid 46310057)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.5 , pp. 1960-1973
    • Davidson, D.1    Schraven, B.2    Veillette, A.3
  • 48
    • 33749515632 scopus 로고    scopus 로고
    • The p110δ isoform of phosphoinositide 3-kinase controls clonal expansion and differentiation of Th cells
    • Okkenhaug, K., D. T. Patton, A. Bilancio, F. Garcon, W. C. Rowan, and B. Vanhaesebroeck. 2006. The p110δ isoform of phosphoinositide 3-kinase controls clonal expansion and differentiation of Th cells. J. Immunol. 177: 5122-5128. (Pubitemid 44527583)
    • (2006) Journal of Immunology , vol.177 , Issue.8 , pp. 5122-5128
    • Okkenhaug, K.1    Patton, D.T.2    Bilancio, A.3    Garcon, F.4    Rowan, W.C.5    Vanhaesebroeck, B.6
  • 49
    • 35348852627 scopus 로고    scopus 로고
    • Distinct signaling mechanisms activate the target of rapamycin in response to different B-cell stimuli
    • Donahue, A. C., and D. A. Fruman. 2007. Distinct signaling mechanisms activate the target of rapamycin in response to different B-cell stimuli. Eur. J. Immunol. 37: 2923-2936.
    • (2007) Eur. J. Immunol. , vol.37 , pp. 2923-2936
    • Donahue, A.C.1    Fruman, D.A.2


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