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Volumn 15, Issue 8, 2005, Pages 702-713

Rheb binds and regulates the mTOR kinase

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA; RAPTORES;

EID: 18044381192     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2005.02.053     Document Type: Article
Times cited : (814)

References (46)
  • 1
    • 0037312507 scopus 로고    scopus 로고
    • Tor signalling in bugs, brain and brawn
    • E. Jacinto, and M.N. Hall Tor signalling in bugs, brain and brawn Nat. Rev. Mol. Cell Biol. 4 2003 117 126
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 117-126
    • Jacinto, E.1    Hall, M.N.2
  • 2
    • 11144300980 scopus 로고    scopus 로고
    • Regulation of cell growth and proliferation in metazoans by mTOR and p70S6 kinase
    • R. Bradshaw E. Dennis Elsevier Science NSA San Diego
    • J. Avruch Regulation of cell growth and proliferation in metazoans by mTOR and p70S6 kinase R. Bradshaw E. Dennis Handbook of Cell Signaling, 2003 Elsevier Science NSA San Diego 523 534
    • (2003) Handbook of Cell Signaling , pp. 523-534
    • Avruch, J.1
  • 6
    • 0037623417 scopus 로고    scopus 로고
    • GβL, a positive regulator of the rapamycin sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • D.H. Kim, D.D. Sarbassov, S.M. Ali, R.R. Latek, K.V.P. Guntur, H. Erdjument-Bromage, P. Tempst, and D.M. Sabatini GβL, 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.P.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 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
    • D. Sarbassov, S.M. Ali, D.H. Kim, D.A. Guertin, R.R. Latek, H. Erdjument-Bromage, P. Tempst, and D.M. Sabatini Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton Curr. Biol. 14 2004 1296 1302
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, 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
  • 9
    • 0035312747 scopus 로고    scopus 로고
    • Regulation of translational initiation by FRAP/mTOR
    • A.C. Gingras, B. Raught, and N. Sonenberg Regulation of translational initiation by FRAP/mTOR Genes Dev. 15 2001 807 826
    • (2001) Genes Dev. , vol.15 , pp. 807-826
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 10
    • 0033607531 scopus 로고    scopus 로고
    • Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro
    • S. Isotani, K. Hara, C. Tokunaga, H. Inoue, J. Avruch, and K. Yonezawa Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro J. Biol. Chem. 274 1999 34493 34498
    • (1999) J. Biol. Chem. , vol.274 , pp. 34493-34498
    • Isotani, S.1    Hara, K.2    Tokunaga, C.3    Inoue, H.4    Avruch, J.5    Yonezawa, K.6
  • 11
    • 2342545519 scopus 로고    scopus 로고
    • Target of rapamycin (TOR): An integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression
    • D.C. Fingar, and J. Blenis Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression Oncogene 23 2004 3151 3171
    • (2004) Oncogene , vol.23 , pp. 3151-3171
    • Fingar, D.C.1    Blenis, J.2
  • 12
    • 0037507252 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) partner, raptor, binds the p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif
    • H. Nojima, C. Tokunaga, S. Eguchi, N. Oshiro, S. Hidayat, K. Yoshino, K. Hara, J. Avruch, and K. Yonezawa The mammalian target of rapamycin (mTOR) partner, raptor, binds the p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif J. Biol. Chem. 278 2003 15461 15464
    • (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    Avruch, J.8    Yonezawa, K.9
  • 13
    • 0037117409 scopus 로고    scopus 로고
    • Identification of a conserved motif required for mTOR signaling
    • S.S. Schalm, and J. Blenis Identification of a conserved motif required for mTOR signaling Curr. Biol. 8 2002 632 639
    • (2002) Curr. Biol. , vol.8 , pp. 632-639
    • Schalm, S.S.1    Blenis, J.2
  • 14
    • 0037718389 scopus 로고    scopus 로고
    • TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation function
    • S.S. Schalm, D.C. Fingar, D.M. Sabatini, and J. Blenis TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation function Curr. Biol. 13 2003 797 806
    • (2003) Curr. Biol. , vol.13 , pp. 797-806
    • Schalm, S.S.1    Fingar, D.C.2    Sabatini, D.M.3    Blenis, J.4
  • 15
    • 0038482156 scopus 로고    scopus 로고
    • Two motifs in the translational repressor PHAS-I required for efficient phosphorylation by mammalian target of rapamycin and for recognition by raptor
    • K.M. Choi, L.P. McMahon, and J.C. Lawrence Jr. Two motifs in the translational repressor PHAS-I required for efficient phosphorylation by mammalian target of rapamycin and for recognition by raptor J. Biol. Chem. 278 2003 19667 19673
    • (2003) J. Biol. Chem. , vol.278 , pp. 19667-19673
    • Choi, K.M.1    McMahon, L.P.2    Lawrence Jr., J.C.3
  • 16
    • 0142071830 scopus 로고    scopus 로고
    • Target of rapamycin (TOR)-signaling and RAIP motifs play distinct roles in mammalian TOR-dependent phosphorylation of initiation factor 4E-binding
    • A. Beugnet, X. Wang, and C.G. Proud Target of rapamycin (TOR)-signaling and RAIP motifs play distinct roles in mammalian TOR-dependent phosphorylation of initiation factor 4E-binding J. Biol. Chem. 278 2003 40717 40722
    • (2003) J. Biol. Chem. , vol.278 , pp. 40717-40722
    • Beugnet, A.1    Wang, X.2    Proud, C.G.3
  • 17
    • 0037126596 scopus 로고    scopus 로고
    • RTG-dependent mitochondria to nucleus signaling is negatively regulated by WD-repeat protein LST8p
    • Z. Liu, T. Sekito, C.B. Epstein, and R.A. Butow RTG-dependent mitochondria to nucleus signaling is negatively regulated by WD-repeat protein LST8p EMBO J. 20 2001 7209 7219
    • (2001) EMBO J. , vol.20 , pp. 7209-7219
    • Liu, Z.1    Sekito, T.2    Epstein, C.B.3    Butow, R.A.4
  • 18
    • 0041758428 scopus 로고    scopus 로고
    • Tuberous sclerosis: From tubers to mTOR
    • D.J. Kwiatkowski Tuberous sclerosis: from tubers to mTOR Ann. Hum. Genet. 67 2003 87 96
    • (2003) Ann. Hum. Genet. , vol.67 , pp. 87-96
    • Kwiatkowski, D.J.1
  • 19
    • 0037306190 scopus 로고    scopus 로고
    • Insulin/IGF and target of rapamycin signaling: A TOR de force in growth control
    • S. Oldham, and E. Hafen Insulin/IGF and target of rapamycin signaling: a TOR de force in growth control Trends Cell Biol. 13 2003 79 85
    • (2003) Trends Cell Biol. , vol.13 , pp. 79-85
    • Oldham, S.1    Hafen, E.2
  • 20
    • 0141923009 scopus 로고    scopus 로고
    • Integration of growth factor and nutrient signaling: Implications for cancer
    • A.F. Shamji, P. Nghiem, and S.L. Schreiber Integration of growth factor and nutrient signaling: implications for cancer Mol. Cell 12 2003 271 280
    • (2003) Mol. Cell , vol.12 , pp. 271-280
    • Shamji, A.F.1    Nghiem, P.2    Schreiber, S.L.3
  • 22
    • 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
    • B.D. Manning, A.R. Tee, M.M. Logsdon, J. Blenis, and L.C. Cantley 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.M.3    Blenis, J.4    Cantley, L.C.5
  • 23
    • 0036714127 scopus 로고    scopus 로고
    • Akt regulates growth by directly phosphorylating Tsc2
    • C.J. Potter, L.G. Pedraza, and T. Xu Akt regulates growth by directly phosphorylating Tsc2 Nat. Cell Biol. 4 2002 658 665
    • (2002) Nat. Cell Biol. , vol.4 , pp. 658-665
    • Potter, C.J.1    Pedraza, L.G.2    Xu, T.3
  • 24
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signal
    • K. Inoki, Y. Li, T. Zhu, J. Wu, and K.L. Guan TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signal 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
  • 25
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • K. Inoki, T. Zhu, and K.L. Guan 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
  • 26
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • Y. Zhang, X. Gao, L.J. Saucedo, B. Ru, B.A. Edgar, and D. Pan 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
  • 29
    • 0041356888 scopus 로고    scopus 로고
    • Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase a rapamycin- and farnesylation-dependent manner
    • A.F. Castro, J.F. Rebhun, G.J. Clark, and L.A. Quilliam Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase a rapamycin- and farnesylation-dependent manner J. Biol. Chem. 278 2003 32493 32496
    • (2003) J. Biol. Chem. , vol.278 , pp. 32493-32496
    • Castro, A.F.1    Rebhun, J.F.2    Clark, G.J.3    Quilliam, L.A.4
  • 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
    • A.R. Tee, B.D. Manning, P.P. Roux, L.C. Cantley, and J. Blenis 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
  • 31
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 Gap activity and regulates mTOR signaling
    • K. Inoki, Y. Li, T. Xu, and K.L. Guan Rheb GTPase is a direct target of TSC2 Gap activity and regulates mTOR signaling Genes Dev. 17 2003 1829 1834
    • (2003) Genes Dev. , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.L.4
  • 32
    • 0038643484 scopus 로고    scopus 로고
    • Rheb promotes cell growth as a component of the insulin/TOR signalling network
    • L.J. Saucedo, X. Gao, D.A. Chiarelli, L. Li, D. Pan, and B.A. Edgar 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
  • 34
    • 0031039427 scopus 로고    scopus 로고
    • Rheb interacts with Raf-1 kinase and may function to integrate growth factor- and protein kinase A-dependent signals
    • W.M. Yee, and P.F. Worley Rheb interacts with Raf-1 kinase and may function to integrate growth factor- and protein kinase A-dependent signals Mol. Cell. Biol. 17 1997 921 933
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 921-933
    • Yee, W.M.1    Worley, P.F.2
  • 36
    • 0030888163 scopus 로고    scopus 로고
    • The Ras-related protein Rheb is farnesylated and antagonizes ras signaling and transformation
    • G.J. Clark, M.S. Kinch, K. Rogers-Graham, S.M. Sebti, A.D. Hamilton, and C.J. Der The Ras-related protein Rheb is farnesylated and antagonizes ras signaling and transformation J. Biol. Chem. 272 1997 10608 10615
    • (1997) J. Biol. Chem. , vol.272 , pp. 10608-10615
    • Clark, G.J.1    Kinch, M.S.2    Rogers-Graham, K.3    Sebti, S.M.4    Hamilton, A.D.5    Der, C.J.6
  • 37
    • 0023715225 scopus 로고
    • Inhibition of NIH 3T3 cell proliferation by mutant ras protein with preference for GDP
    • L.A. Feig, and G.M. Cooper Inhibition of NIH 3T3 cell proliferation by mutant ras protein with preference for GDP Mol. Cell. Biol. 8 1988 3235 3243
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3235-3243
    • Feig, L.A.1    Cooper, G.M.2
  • 38
    • 0034051278 scopus 로고    scopus 로고
    • Loss of Rhb1, a Rheb-related GTPase in fission yeast, causes growth arrest with a terminal phenotype similar to that caused by nitrogen starvation
    • K.E. Mach, K.A. Furge, and C.F. Albright Loss of Rhb1, a Rheb-related GTPase in fission yeast, causes growth arrest with a terminal phenotype similar to that caused by nitrogen starvation Genetics 155 2000 611 622
    • (2000) Genetics , vol.155 , pp. 611-622
    • MacH, K.E.1    Furge, K.A.2    Albright, C.F.3
  • 39
    • 0141925647 scopus 로고    scopus 로고
    • Identification of dominant negative mutants of Rheb GTPase and their use of involvement of human Rheb in the activation of p70S6K
    • A.P. Tabancay Jr., C.L. Gau, I.M. Machado, E.J. Uhlmann, D.H. Gutmann, L. Guo, and F. Tamanoi Identification of dominant negative mutants of Rheb GTPase and their use of involvement of human Rheb in the activation of p70S6K J. Biol. Chem. 278 2003 39921 39930
    • (2003) J. Biol. Chem. , vol.278 , pp. 39921-39930
    • Tabancay Jr., A.P.1    Gau, C.L.2    MacHado, I.M.3    Uhlmann, E.J.4    Gutmann, D.H.5    Guo, L.6    Tamanoi, F.7
  • 40
    • 4444276510 scopus 로고    scopus 로고
    • Biochemical and functional characterizations of small GTPase Rheb and TSC2 GAP activity
    • Y. Li, K. Inoki, and K.L. Guan Biochemical and functional characterizations of small GTPase Rheb and TSC2 GAP activity Mol. Cell. Biol. 24 2004 7965 7975
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7965-7975
    • Li, Y.1    Inoki, K.2    Guan, K.L.3
  • 43
    • 0027956706 scopus 로고
    • Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues
    • E. Chuang, D. Barnard, L. Hettich, X.F. Zhang, J. Avruch, and M.S. Marshall Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues Mol. Cell. Biol. 14 1994 5318 5325
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5318-5325
    • Chuang, E.1    Barnard, D.2    Hettich, L.3    Zhang, X.F.4    Avruch, J.5    Marshall, M.S.6
  • 46
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • K. Hara, K. Yonezawa, Q.P. Weng, M.T. Kozlowski, C. Belham, and J. Avruch Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism J. Biol. Chem. 273 1998 14484 14494
    • (1998) J. Biol. Chem. , vol.273 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6


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