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Volumn 14, Issue 1, 2013, Pages

mTOR direct interactions with Rheb-GTPase and raptor: Sub-cellular localization using fluorescence lifetime imaging

Author keywords

FLIM; FRET; GFP; mTOR; Raptor; Rheb

Indexed keywords

BINDING PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; RED FLUORESCENT PROTEIN; REGULATORY ASSOCIATED PROTEIN OF MAMMALIAN TARGET OF RAPAMYCIN; RHEB PROTEIN; UNCLASSIFIED DRUG;

EID: 84872141223     PISSN: None     EISSN: 14712121     Source Type: Journal    
DOI: 10.1186/1471-2121-14-3     Document Type: Article
Times cited : (54)

References (42)
  • 1
    • 14844363721 scopus 로고    scopus 로고
    • Signaling by target of rapamycin proteins in cell growth control
    • 10.1128/MMBR.69.1.79-100.2005, 1082789, 15755954
    • Inoki K, Ouyang H, Li Y, Guan KL. Signaling by target of rapamycin proteins in cell growth control. Microbiol Mol Biol Rev 2005, 69:79-100. 10.1128/MMBR.69.1.79-100.2005, 1082789, 15755954.
    • (2005) Microbiol Mol Biol Rev , vol.69 , pp. 79-100
    • Inoki, K.1    Ouyang, H.2    Li, Y.3    Guan, K.L.4
  • 2
    • 0037178781 scopus 로고    scopus 로고
    • Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action
    • 10.1016/S0092-8674(02)00833-4, 12150926
    • Hara K, Maruki Y, Long X, Yoshino K, Oshiro N, Hidayat S, Tokunaga C, Avruch J, Yonezawa K. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 2002, 110:177-189. 10.1016/S0092-8674(02)00833-4, 12150926.
    • (2002) Cell , vol.110 , pp. 177-189
    • Hara, K.1    Maruki, Y.2    Long, X.3    Yoshino, K.4    Oshiro, N.5    Hidayat, S.6    Tokunaga, C.7    Avruch, J.8    Yonezawa, K.9
  • 3
    • 0037178786 scopus 로고    scopus 로고
    • MTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • 10.1016/S0092-8674(02)00808-5, 12150925
    • Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 2002, 110:163-175. 10.1016/S0092-8674(02)00808-5, 12150925.
    • (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
  • 4
    • 43249124698 scopus 로고    scopus 로고
    • PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis
    • 10.1371/journal.pone.0001217, 2075366, 18030348
    • Thedieck K, Polak P, Kim ML, Molle KD, Cohen A, Jeno P, Arrieumerlou C, Hall MN. PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis. PLoS One 2007, 2:e1217. 10.1371/journal.pone.0001217, 2075366, 18030348.
    • (2007) PLoS One , vol.2
    • Thedieck, K.1    Polak, P.2    Kim, M.L.3    Molle, K.D.4    Cohen, A.5    Jeno, P.6    Arrieumerlou, C.7    Hall, M.N.8
  • 5
    • 33750058023 scopus 로고    scopus 로고
    • Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?
    • 10.1038/sj.onc.1209885, 17041621
    • Corradetti MN, Guan KL. Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?. Oncogene 2006, 25:6347-6360. 10.1038/sj.onc.1209885, 17041621.
    • (2006) Oncogene , vol.25 , pp. 6347-6360
    • Corradetti, M.N.1    Guan, K.L.2
  • 6
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • 10.1016/j.cub.2004.06.054, 15268862
    • Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol 2004, 14:1296-1302. 10.1016/j.cub.2004.06.054, 15268862.
    • (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
  • 7
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • 10.1038/ncb1183, 15467718
    • Jacinto E, Loewith R, Schmidt A, Lin S, Ruegg MA, Hall A, Hall MN. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat Cell Biol 2004, 6:1122-1128. 10.1038/ncb1183, 15467718.
    • (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
  • 8
    • 33749076673 scopus 로고    scopus 로고
    • SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity
    • 10.1016/j.cell.2006.08.033, 16962653
    • Jacinto E, Facchinetti V, Liu D, Soto N, Wei S, Jung SY, Huang Q, Qin J, Su B. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell 2006, 127:125-137. 10.1016/j.cell.2006.08.033, 16962653.
    • (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
  • 10
    • 0041827366 scopus 로고    scopus 로고
    • Drosophila Rheb GTPase is required for cell cycle progression and cell growth
    • 10.1242/jcs.00661, 12893813
    • Patel PH, Thapar N, Guo L, Martinez M, Maris J, Gau CL, Lengyel JA, Tamanoi F. Drosophila Rheb GTPase is required for cell cycle progression and cell growth. J Cell Sci 2003, 116:3601-3610. 10.1242/jcs.00661, 12893813.
    • (2003) J Cell Sci , vol.116 , pp. 3601-3610
    • Patel, P.H.1    Thapar, N.2    Guo, L.3    Martinez, M.4    Maris, J.5    Gau, C.L.6    Lengyel, J.A.7    Tamanoi, F.8
  • 11
    • 18044381192 scopus 로고    scopus 로고
    • Rheb binds and regulates the mTOR kinase
    • 10.1016/j.cub.2005.02.053, 15854902
    • Long X, Lin Y, Ortiz-Vega S, Yonezawa K, Avruch J. Rheb binds and regulates the mTOR kinase. Curr Biol 2005, 15:702-713. 10.1016/j.cub.2005.02.053, 15854902.
    • (2005) Curr Biol , vol.15 , pp. 702-713
    • Long, X.1    Lin, Y.2    Ortiz-Vega, S.3    Yonezawa, K.4    Avruch, J.5
  • 12
    • 24044442298 scopus 로고    scopus 로고
    • Analysis of mTOR signaling by the small G-proteins, Rheb and RhebL1
    • 10.1016/j.febslet.2005.07.054, 16098514
    • Tee AR, Blenis J, Proud CG. Analysis of mTOR signaling by the small G-proteins, Rheb and RhebL1. FEBS Lett 2005, 579:4763-4768. 10.1016/j.febslet.2005.07.054, 16098514.
    • (2005) FEBS Lett , vol.579 , pp. 4763-4768
    • Tee, A.R.1    Blenis, J.2    Proud, C.G.3
  • 13
    • 0346366446 scopus 로고    scopus 로고
    • Raptor, a binding partner of target of rapamycin
    • 10.1016/j.bbrc.2003.07.018, 14684181
    • Yonezawa K, Tokunaga C, Oshiro N, Yoshino K. Raptor, a binding partner of target of rapamycin. Biochem Biophys Res Commun 2004, 313:437-441. 10.1016/j.bbrc.2003.07.018, 14684181.
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 437-441
    • Yonezawa, K.1    Tokunaga, C.2    Oshiro, N.3    Yoshino, K.4
  • 14
    • 0037507252 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif
    • 10.1074/jbc.C200665200, 12604610
    • Nojima H, Tokunaga C, Eguchi S, Oshiro N, Hidayat S, Yoshino K, Hara K, Tanaka N, Avruch J, Yonezawa K. The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif. J Biol Chem 2003, 278:15461-15464. 10.1074/jbc.C200665200, 12604610.
    • (2003) J Biol Chem , vol.278 , pp. 15461-15464
    • Nojima, H.1    Tokunaga, C.2    Eguchi, S.3    Oshiro, N.4    Hidayat, S.5    Yoshino, K.6    Hara, K.7    Tanaka, N.8    Avruch, J.9    Yonezawa, K.10
  • 15
    • 25444471326 scopus 로고    scopus 로고
    • The use of time-resolved fluorescence imaging in the study of protein kinase C localisation in cells
    • 10.1186/1471-2121-6-22, 1131895, 15854225
    • Stubbs CD, Botchway SW, Slater SJ, Parker AW. The use of time-resolved fluorescence imaging in the study of protein kinase C localisation in cells. BMC Cell Biol 2005, 6:22. 10.1186/1471-2121-6-22, 1131895, 15854225.
    • (2005) BMC Cell Biol , vol.6 , pp. 22
    • Stubbs, C.D.1    Botchway, S.W.2    Slater, S.J.3    Parker, A.W.4
  • 16
    • 67649887900 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of interactions between Golgi tethering factors and small GTPases in plants
    • 10.1111/j.1600-0854.2009.00930.x, 19490533
    • Osterrieder A, Carvalho CM, Latijnhouwers M, Johansen JN, Stubbs C, Botchway S, Hawes C. Fluorescence lifetime imaging of interactions between Golgi tethering factors and small GTPases in plants. Traffic 2009, 10:1034-1046. 10.1111/j.1600-0854.2009.00930.x, 19490533.
    • (2009) Traffic , vol.10 , pp. 1034-1046
    • Osterrieder, A.1    Carvalho, C.M.2    Latijnhouwers, M.3    Johansen, J.N.4    Stubbs, C.5    Botchway, S.6    Hawes, C.7
  • 17
    • 77953177103 scopus 로고    scopus 로고
    • Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties
    • 10.1105/tpc.110.074385, 2879755, 20424177
    • Sparkes I, Tolley N, Aller I, Svozil J, Osterrieder A, Botchway S, Mueller C, Frigerio L, Hawes C. Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties. Plant Cell 2010, 22:1333-1343. 10.1105/tpc.110.074385, 2879755, 20424177.
    • (2010) Plant Cell , vol.22 , pp. 1333-1343
    • Sparkes, I.1    Tolley, N.2    Aller, I.3    Svozil, J.4    Osterrieder, A.5    Botchway, S.6    Mueller, C.7    Frigerio, L.8    Hawes, C.9
  • 18
  • 19
    • 0037057801 scopus 로고    scopus 로고
    • The nuclear phosphoinositide 3-kinase/AKT pathway: a new second messenger system
    • 10.1016/S1388-1981(02)00300-1, 12385889
    • Neri LM, Borgatti P, Capitani S, Martelli AM. The nuclear phosphoinositide 3-kinase/AKT pathway: a new second messenger system. Biochim Biophys Acta 2002, 1584:73-80. 10.1016/S1388-1981(02)00300-1, 12385889.
    • (2002) Biochim Biophys Acta , vol.1584 , pp. 73-80
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 20
    • 27944467785 scopus 로고    scopus 로고
    • "New"-clear functions of PDK1: beyond a master kinase in the cytosol?
    • 10.1002/jcb.20651, 16187290
    • Kikani CK, Dong LQ, Liu F. "New"-clear functions of PDK1: beyond a master kinase in the cytosol?. J Cell Biochem 2005, 96:1157-1162. 10.1002/jcb.20651, 16187290.
    • (2005) J Cell Biochem , vol.96 , pp. 1157-1162
    • Kikani, C.K.1    Dong, L.Q.2    Liu, F.3
  • 21
    • 0034647674 scopus 로고    scopus 로고
    • Translocation of Akt/PKB to the nucleus of osteoblast-like MC3T3-E1 cells exposed to proliferative growth factors
    • 10.1016/S0014-5793(00)01758-0, 10899305
    • Borgatti P, Martelli AM, Bellacosa A, Casto R, Massari L, Capitani S, Neri LM. Translocation of Akt/PKB to the nucleus of osteoblast-like MC3T3-E1 cells exposed to proliferative growth factors. FEBS Lett 2000, 477:27-32. 10.1016/S0014-5793(00)01758-0, 10899305.
    • (2000) FEBS Lett , vol.477 , pp. 27-32
    • Borgatti, P.1    Martelli, A.M.2    Bellacosa, A.3    Casto, R.4    Massari, L.5    Capitani, S.6    Neri, L.M.7
  • 22
    • 27844535741 scopus 로고    scopus 로고
    • Class reunion: PTEN joins the nuclear crew
    • 10.1038/sj.onc.1209089, 16288286
    • Lian Z, Di Cristofano A. Class reunion: PTEN joins the nuclear crew. Oncogene 2005, 24:7394-7400. 10.1038/sj.onc.1209089, 16288286.
    • (2005) Oncogene , vol.24 , pp. 7394-7400
    • Lian, Z.1    Di Cristofano, A.2
  • 23
    • 33846475008 scopus 로고    scopus 로고
    • Akt regulates nuclear/cytoplasmic localization of tuberin
    • 10.1038/sj.onc.1209812, 16862180
    • Rosner M, Freilinger A, Hengstschlager M. Akt regulates nuclear/cytoplasmic localization of tuberin. Oncogene 2007, 26:521-531. 10.1038/sj.onc.1209812, 16862180.
    • (2007) Oncogene , vol.26 , pp. 521-531
    • Rosner, M.1    Freilinger, A.2    Hengstschlager, M.3
  • 24
    • 0031590007 scopus 로고    scopus 로고
    • Insulin stimulates p70 S6 kinase in the nucleus of cells
    • 10.1006/bbrc.1997.6699, 9175775
    • Kim SJ, Kahn CR. Insulin stimulates p70 S6 kinase in the nucleus of cells. Biochem Biophys Res Commun 1997, 234:681-685. 10.1006/bbrc.1997.6699, 9175775.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 681-685
    • Kim, S.J.1    Kahn, C.R.2
  • 25
    • 0034687688 scopus 로고    scopus 로고
    • Cytoplasmic-nuclear shuttling of FKBP12-rapamycin-associated protein is involved in rapamycin-sensitive signaling and translation initiation
    • 10.1073/pnas.011511898, 18920, 11114166
    • Kim JE, Chen J. Cytoplasmic-nuclear shuttling of FKBP12-rapamycin-associated protein is involved in rapamycin-sensitive signaling and translation initiation. Proc Natl Acad Sci U S A 2000, 97:14340-14345. 10.1073/pnas.011511898, 18920, 11114166.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14340-14345
    • Kim, J.E.1    Chen, J.2
  • 26
    • 0037008730 scopus 로고    scopus 로고
    • Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture
    • 10.1074/jbc.M202625200, 12000755
    • Zhang X, Shu L, Hosoi H, Murti KG, Houghton PJ. Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture. J Biol Chem 2002, 277:28127-28134. 10.1074/jbc.M202625200, 12000755.
    • (2002) J Biol Chem , vol.277 , pp. 28127-28134
    • Zhang, X.1    Shu, L.2    Hosoi, H.3    Murti, K.G.4    Houghton, P.J.5
  • 27
    • 52949137425 scopus 로고    scopus 로고
    • Cytoplasmic and nuclear distribution of the protein complexes mTORC1 and mTORC2: rapamycin triggers dephosphorylation and delocalization of the mTORC2 components rictor and sin1
    • 10.1093/hmg/ddn192, 18614546
    • Rosner M, Hengstschlager M. Cytoplasmic and nuclear distribution of the protein complexes mTORC1 and mTORC2: rapamycin triggers dephosphorylation and delocalization of the mTORC2 components rictor and sin1. Hum Mol Genet 2008, 17:2934-2948. 10.1093/hmg/ddn192, 18614546.
    • (2008) Hum Mol Genet , vol.17 , pp. 2934-2948
    • Rosner, M.1    Hengstschlager, M.2
  • 28
    • 33646143793 scopus 로고    scopus 로고
    • Localization of Rheb to the endomembrane is critical for its signaling function
    • 10.1016/j.bbrc.2006.03.220, 16631613
    • Buerger C, DeVries B, Stambolic V. Localization of Rheb to the endomembrane is critical for its signaling function. Biochem Biophys Res Commun 2006, 344:869-880. 10.1016/j.bbrc.2006.03.220, 16631613.
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 869-880
    • Buerger, C.1    DeVries, B.2    Stambolic, V.3
  • 29
    • 52949126962 scopus 로고    scopus 로고
    • Constitutively active Rheb induces oncogenic transformation
    • 10.1038/onc.2008.180, 2562864, 18521078
    • Jiang H, Vogt PK. Constitutively active Rheb induces oncogenic transformation. Oncogene 2008, 27:5729-5740. 10.1038/onc.2008.180, 2562864, 18521078.
    • (2008) Oncogene , vol.27 , pp. 5729-5740
    • Jiang, H.1    Vogt, P.K.2
  • 30
    • 84872616594 scopus 로고    scopus 로고
    • Differential requirement of CAAX-mediated posttranslational processing for Rheb localization and signaling
    • Hanker AB, Mitin N, Wilder RS, Henske EP, Tamanoi F, Cox AD, Der CJ. Differential requirement of CAAX-mediated posttranslational processing for Rheb localization and signaling. Oncogene 2009, 19:19.
    • (2009) Oncogene , vol.19 , pp. 19
    • Hanker, A.B.1    Mitin, N.2    Wilder, R.S.3    Henske, E.P.4    Tamanoi, F.5    Cox, A.D.6    Der, C.J.7
  • 31
    • 66349138676 scopus 로고    scopus 로고
    • Nutrient control of TORC1, a cell-cycle regulator
    • 10.1016/j.tcb.2009.03.005, 19419870
    • Wang X, Proud CG. Nutrient control of TORC1, a cell-cycle regulator. Trends Cell Biol 2009, 19:260-267. 10.1016/j.tcb.2009.03.005, 19419870.
    • (2009) Trends Cell Biol , vol.19 , pp. 260-267
    • Wang, X.1    Proud, C.G.2
  • 32
    • 54449097914 scopus 로고    scopus 로고
    • The switch I region of Rheb is critical for its interaction with FKBP38
    • 10.1074/jbc.M802356200, 2533802, 18658153
    • Ma D, Bai X, Guo S, Jiang Y. The switch I region of Rheb is critical for its interaction with FKBP38. J Biol Chem 2008, 283:25963-25970. 10.1074/jbc.M802356200, 2533802, 18658153.
    • (2008) J Biol Chem , vol.283 , pp. 25963-25970
    • Ma, D.1    Bai, X.2    Guo, S.3    Jiang, Y.4
  • 33
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • 10.1126/science.1157535, 2475333, 18497260
    • Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, Bar-Peled L, Sabatini DM. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 2008, 320:1496-1501. 10.1126/science.1157535, 2475333, 18497260.
    • (2008) Science , vol.320 , 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
  • 34
    • 25444450400 scopus 로고    scopus 로고
    • Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway
    • 10.1074/jbc.M506280200, 16046393
    • Takahashi K, Nakagawa M, Young SG, Yamanaka S. Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway. J Biol Chem 2005, 280:32768-32774. 10.1074/jbc.M506280200, 16046393.
    • (2005) J Biol Chem , vol.280 , pp. 32768-32774
    • Takahashi, K.1    Nakagawa, M.2    Young, S.G.3    Yamanaka, S.4
  • 35
    • 0346422440 scopus 로고    scopus 로고
    • FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus
    • Drenan RM, Liu X, Bertram PG, Zheng XF. FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus. J Biol Chem 2004, 279:772-778.
    • (2004) J Biol Chem , vol.279 , pp. 772-778
    • Drenan, R.M.1    Liu, X.2    Bertram, P.G.3    Zheng, X.F.4
  • 36
    • 27944452168 scopus 로고    scopus 로고
    • Identification of novel single amino acid changes that result in hyperactivation of the unique GTPase, Rheb, in fission yeast
    • 10.1111/j.1365-2958.2005.04877.x, 16262791
    • Urano J, Comiso MJ, Guo L, Aspuria PJ, Deniskin R, Tabancay AP, Kato-Stankiewicz J, Tamanoi F. Identification of novel single amino acid changes that result in hyperactivation of the unique GTPase, Rheb, in fission yeast. Mol Microbiol 2005, 58:1074-1086. 10.1111/j.1365-2958.2005.04877.x, 16262791.
    • (2005) Mol Microbiol , vol.58 , pp. 1074-1086
    • Urano, J.1    Comiso, M.J.2    Guo, L.3    Aspuria, P.J.4    Deniskin, R.5    Tabancay, A.P.6    Kato-Stankiewicz, J.7    Tamanoi, F.8
  • 37
    • 77953091045 scopus 로고    scopus 로고
    • Structure of the human mTOR complex I and its implications for rapamycin inhibition
    • 10.1016/j.molcel.2010.05.017, 2887672, 20542007
    • Yip CK, Murata K, Walz T, Sabatini DM, Kang SA. Structure of the human mTOR complex I and its implications for rapamycin inhibition. Mol Cell 2010, 38:768-774. 10.1016/j.molcel.2010.05.017, 2887672, 20542007.
    • (2010) Mol Cell , vol.38 , pp. 768-774
    • Yip, C.K.1    Murata, K.2    Walz, T.3    Sabatini, D.M.4    Kang, S.A.5
  • 38
    • 21244480367 scopus 로고    scopus 로고
    • The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses
    • 10.1074/jbc.M414499200, 15772076
    • Smith EM, Finn SG, Tee AR, Browne GJ, Proud CG. The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses. J Biol Chem 2005, 280:18717-18727. 10.1074/jbc.M414499200, 15772076.
    • (2005) J Biol Chem , vol.280 , pp. 18717-18727
    • Smith, E.M.1    Finn, S.G.2    Tee, A.R.3    Browne, G.J.4    Proud, C.G.5
  • 39
    • 1942487890 scopus 로고    scopus 로고
    • Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function
    • 10.1111/j.1356-9597.2004.00727.x, 15066126
    • Oshiro N, Yoshino K, Hidayat S, Tokunaga C, Hara K, Eguchi S, Avruch J, Yonezawa K. Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function. Genes Cells 2004, 9:359-366. 10.1111/j.1356-9597.2004.00727.x, 15066126.
    • (2004) Genes Cells , vol.9 , pp. 359-366
    • Oshiro, N.1    Yoshino, K.2    Hidayat, S.3    Tokunaga, C.4    Hara, K.5    Eguchi, S.6    Avruch, J.7    Yonezawa, K.8
  • 40
    • 77950900079 scopus 로고    scopus 로고
    • MTOR Ser-2481 autophosphorylation monitors mTORC-specific catalytic activity and clarifies rapamycin mechanism of action
    • 2832937, 20022946
    • Soliman GA, Acosta-Jaquez HA, Dunlop EA, Ekim B, Maj NE, Tee AR, Fingar DC. mTOR Ser-2481 autophosphorylation monitors mTORC-specific catalytic activity and clarifies rapamycin mechanism of action. J Biol Chem 2009, 285:7866-7879. 2832937, 20022946.
    • (2009) J Biol Chem , vol.285 , pp. 7866-7879
    • Soliman, G.A.1    Acosta-Jaquez, H.A.2    Dunlop, E.A.3    Ekim, B.4    Maj, N.E.5    Tee, A.R.6    Fingar, D.C.7
  • 41
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase
    • Zoncu R, Bar-Peled L, Efeyan A, Wang S, Sancak Y, Sabatini DM. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science (New York, NY) 334:678-683.
    • Science (New York, NY) , vol.334 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6
  • 42
    • 34147133469 scopus 로고    scopus 로고
    • SnapShot: mTOR signaling
    • Soulard A, Hall MN. SnapShot: mTOR signaling. Cell 2007, 129:434.
    • (2007) Cell , vol.129 , pp. 434
    • Soulard, A.1    Hall, M.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.