메뉴 건너뛰기




Volumn 68, Issue 3, 2017, Pages 552-565.e8

Intersubunit Crosstalk in the Rag GTPase Heterodimer Enables mTORC1 to Respond Rapidly to Amino Acid Availability

Author keywords

amino acid sensing; enzymatic mechanism; mTORC1; negative cooperativity; Rag GTPases

Indexed keywords

AMINO ACID; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; HETERODIMER; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; RAG GTPASE; UNCLASSIFIED DRUG; MONOMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN BINDING; RRAGA PROTEIN, HUMAN; RRAGC PROTEIN, HUMAN;

EID: 85031798280     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2017.09.026     Document Type: Article
Times cited : (67)

References (47)
  • 2
    • 84889597180 scopus 로고    scopus 로고
    • Longin and GAF domains: structural evolution and adaptation to the subcellular trafficking machinery
    • De Franceschi, N., Wild, K., Schlacht, A., Dacks, J.B., Sinning, I., Filippini, F., Longin and GAF domains: structural evolution and adaptation to the subcellular trafficking machinery. Traffic 15 (2014), 104–121.
    • (2014) Traffic , vol.15 , pp. 104-121
    • De Franceschi, N.1    Wild, K.2    Schlacht, A.3    Dacks, J.B.4    Sinning, I.5    Filippini, F.6
  • 3
    • 84878532557 scopus 로고    scopus 로고
    • Signal integration by mTORC1 coordinates nutrient input with biosynthetic output
    • Dibble, C.C., Manning, B.D., Signal integration by mTORC1 coordinates nutrient input with biosynthetic output. Nat. Cell Biol. 15 (2013), 555–564.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 555-564
    • Dibble, C.C.1    Manning, B.D.2
  • 4
    • 84922789990 scopus 로고    scopus 로고
    • Nutrient-sensing mechanisms and pathways
    • Efeyan, A., Comb, W.C., Sabatini, D.M., Nutrient-sensing mechanisms and pathways. Nature 517 (2015), 302–310.
    • (2015) Nature , vol.517 , pp. 302-310
    • Efeyan, A.1    Comb, W.C.2    Sabatini, D.M.3
  • 5
    • 0023715225 scopus 로고
    • Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP
    • Feig, L.A., Cooper, G.M., Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity 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
  • 6
    • 0003818541 scopus 로고    scopus 로고
    • Structure and Mechanism in Protein Science
    • Macmillan
    • Fersht, A., Structure and Mechanism in Protein Science. 1999, Macmillan.
    • (1999)
    • Fersht, A.1
  • 7
    • 0023664530 scopus 로고
    • Preparation and characterization of nucleotide-free and metal ion-free p21 “apoprotein”
    • Feuerstein, J., Goody, R.S., Wittinghofer, A., Preparation and characterization of nucleotide-free and metal ion-free p21 “apoprotein”. J. Biol. Chem. 262 (1987), 8455–8458.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8455-8458
    • Feuerstein, J.1    Goody, R.S.2    Wittinghofer, A.3
  • 9
    • 80051873144 scopus 로고    scopus 로고
    • Crystal structure of the Gtr1p-Gtr2p complex reveals new insights into the amino acid-induced TORC1 activation
    • Gong, R., Li, L., Liu, Y., Wang, P., Yang, H., Wang, L., Cheng, J., Guan, K.-L., Xu, Y., Crystal structure of the Gtr1p-Gtr2p complex reveals new insights into the amino acid-induced TORC1 activation. Genes Dev. 25 (2011), 1668–1673.
    • (2011) Genes Dev. , vol.25 , pp. 1668-1673
    • Gong, R.1    Li, L.2    Liu, Y.3    Wang, P.4    Yang, H.5    Wang, L.6    Cheng, J.7    Guan, K.-L.8    Xu, Y.9
  • 10
    • 85010505580 scopus 로고    scopus 로고
    • Nutrient sensing and TOR signaling in yeast and mammals
    • González, A., Hall, M.N., Nutrient sensing and TOR signaling in yeast and mammals. EMBO J. 36 (2017), 397–408.
    • (2017) EMBO J. , vol.36 , pp. 397-408
    • González, A.1    Hall, M.N.2
  • 12
    • 0037125971 scopus 로고    scopus 로고
    • The structural basis for the transition from Ras-GTP to Ras-GDP
    • Hall, B.E., Bar-Sagi, D., Nassar, N., The structural basis for the transition from Ras-GTP to Ras-GDP. Proc. Natl. Acad. Sci. USA 99 (2002), 12138–12142.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12138-12142
    • Hall, B.E.1    Bar-Sagi, D.2    Nassar, N.3
  • 13
    • 0023665149 scopus 로고
    • A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein
    • Hwang, Y.W., Miller, D.L., A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein. J. Biol. Chem. 262 (1987), 13081–13085.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13081-13085
    • Hwang, Y.W.1    Miller, D.L.2
  • 14
    • 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., Guan, K.-L., 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
  • 15
    • 84865492819 scopus 로고    scopus 로고
    • Crystal structure of the Gtr1p(GTP)-Gtr2p(GDP) protein complex reveals large structural rearrangements triggered by GTP-to-GDP conversion
    • Jeong, J.-H., Lee, K.-H., Kim, Y.-M., Kim, D.-H., Oh, B.-H., Kim, Y.-G., Crystal structure of the Gtr1p(GTP)-Gtr2p(GDP) protein complex reveals large structural rearrangements triggered by GTP-to-GDP conversion. J. Biol. Chem. 287 (2012), 29648–29653.
    • (2012) J. Biol. Chem. , vol.287 , pp. 29648-29653
    • Jeong, J.-H.1    Lee, K.-H.2    Kim, Y.-M.3    Kim, D.-H.4    Oh, B.-H.5    Kim, Y.-G.6
  • 17
    • 84932638310 scopus 로고    scopus 로고
    • Amino acid-dependent mTORC1 regulation by the lysosomal membrane protein SLC38A9
    • Jung, J., Genau, H.M., Behrends, C., Amino acid-dependent mTORC1 regulation by the lysosomal membrane protein SLC38A9. Mol. Cell. Biol. 35 (2015), 2479–2494.
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 2479-2494
    • Jung, J.1    Genau, H.M.2    Behrends, C.3
  • 18
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe, D.D., Wolf, Y.I., Koonin, E.V., Aravind, L., Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317 (2002), 41–72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 19
    • 84876431000 scopus 로고    scopus 로고
    • Discovery of new Longin and Roadblock domains that form platforms for small GTPases in Ragulator and TRAPP-II
    • Levine, T.P., Daniels, R.D., Wong, L.H., Gatta, A.T., Gerondopoulos, A., Barr, F.A., Discovery of new Longin and Roadblock domains that form platforms for small GTPases in Ragulator and TRAPP-II. Small GTPases 4 (2013), 62–69.
    • (2013) Small GTPases , vol.4 , pp. 62-69
    • Levine, T.P.1    Daniels, R.D.2    Wong, L.H.3    Gatta, A.T.4    Gerondopoulos, A.5    Barr, F.A.6
  • 20
    • 4444276510 scopus 로고    scopus 로고
    • Biochemical and functional characterizations of small GTPase Rheb and TSC2 GAP activity
    • Li, Y., Inoki, K., Guan, K.L., 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
  • 21
    • 84971006595 scopus 로고    scopus 로고
    • De novo RRAGC mutation activates mTORC1 signaling in syndromic fetal dilated cardiomyopathy
    • Long, P.A., Zimmermann, M.T., Kim, M., Evans, J.M., Xu, X., Olson, T.M., De novo RRAGC mutation activates mTORC1 signaling in syndromic fetal dilated cardiomyopathy. Hum. Genet. 135 (2016), 909–917.
    • (2016) Hum. Genet. , vol.135 , pp. 909-917
    • Long, P.A.1    Zimmermann, M.T.2    Kim, M.3    Evans, J.M.4    Xu, X.5    Olson, T.M.6
  • 22
    • 84894114029 scopus 로고    scopus 로고
    • Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome
    • Menon, S., Dibble, C.C., Talbott, G., Hoxhaj, G., Valvezan, A.J., Takahashi, H., Cantley, L.C., Manning, B.D., Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome. Cell 156 (2014), 771–785.
    • (2014) Cell , vol.156 , pp. 771-785
    • Menon, S.1    Dibble, C.C.2    Talbott, G.3    Hoxhaj, G.4    Valvezan, A.J.5    Takahashi, H.6    Cantley, L.C.7    Manning, B.D.8
  • 23
    • 0032771639 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae putative G protein, Gtr1p, which forms complexes with itself and a novel protein designated as Gtr2p, negatively regulates the Ran/Gsp1p G protein cycle through Gtr2p
    • Nakashima, N., Noguchi, E., Nishimoto, T., Saccharomyces cerevisiae putative G protein, Gtr1p, which forms complexes with itself and a novel protein designated as Gtr2p, negatively regulates the Ran/Gsp1p G protein cycle through Gtr2p. Genetics 152 (1999), 853–867.
    • (1999) Genetics , vol.152 , pp. 853-867
    • Nakashima, N.1    Noguchi, E.2    Nishimoto, T.3
  • 24
    • 0023790685 scopus 로고
    • Kinetics of adenosine 5′-triphosphate and adenosine 5′-diphosphate interaction with G-actin
    • Nowak, E., Goody, R.S., Kinetics of adenosine 5′-triphosphate and adenosine 5′-diphosphate interaction with G-actin. Biochemistry 27 (1988), 8613–8617.
    • (1988) Biochemistry , vol.27 , pp. 8613-8617
    • Nowak, E.1    Goody, R.S.2
  • 26
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis
    • Pai, E.F., Krengel, U., Petsko, G.A., Goody, R.S., Kabsch, W., Wittinghofer, A., Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9 (1990), 2351–2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 27
    • 84878353147 scopus 로고    scopus 로고
    • Amino acid deprivation inhibits TORC1 through a GTPase-activating protein complex for the Rag family GTPase Gtr1
    • Panchaud, N., Péli-Gulli, M.-P., De Virgilio, C., Amino acid deprivation inhibits TORC1 through a GTPase-activating protein complex for the Rag family GTPase Gtr1. Sci. Signal., 6, 2013, ra42.
    • (2013) Sci. Signal. , vol.6 , pp. ra42
    • Panchaud, N.1    Péli-Gulli, M.-P.2    De Virgilio, C.3
  • 28
    • 0035909810 scopus 로고    scopus 로고
    • Role of SRP RNA in the GTPase cycles of Ffh and FtsY
    • Peluso, P., Shan, S.-O., Nock, S., Herschlag, D., Walter, P., Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry 40 (2001), 15224–15233.
    • (2001) Biochemistry , vol.40 , pp. 15224-15233
    • Peluso, P.1    Shan, S.-O.2    Nock, S.3    Herschlag, D.4    Walter, P.5
  • 29
    • 84886871016 scopus 로고    scopus 로고
    • Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases
    • Petit, C.S., Roczniak-Ferguson, A., Ferguson, S.M., Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases. J. Cell Biol. 202 (2013), 1107–1122.
    • (2013) J. Cell Biol. , vol.202 , pp. 1107-1122
    • Petit, C.S.1    Roczniak-Ferguson, A.2    Ferguson, S.M.3
  • 31
    • 18244362311 scopus 로고    scopus 로고
    • Novel role of the small GTPase Rheb: its implication in endocytic pathway independent of the activation of mammalian target of rapamycin
    • Saito, K., Araki, Y., Kontani, K., Nishina, H., Katada, T., Novel role of the small GTPase Rheb: its implication in endocytic pathway independent of the activation of mammalian target of rapamycin. J. Biochem. 137 (2005), 423–430.
    • (2005) J. Biochem. , vol.137 , pp. 423-430
    • Saito, K.1    Araki, Y.2    Kontani, K.3    Nishina, H.4    Katada, T.5
  • 33
    • 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., Sabatini, D.M., Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141 (2010), 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
  • 34
    • 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., 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
  • 36
    • 0028849086 scopus 로고
    • Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases
    • Schürmann, A., Brauers, A., Massmann, S., Becker, W., Joost, H.G., Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. J. Biol. Chem. 270 (1995), 28982–28988.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28982-28988
    • Schürmann, A.1    Brauers, A.2    Massmann, S.3    Becker, W.4    Joost, H.G.5
  • 37
    • 84997171453 scopus 로고    scopus 로고
    • ATPase and GTPase tangos drive intracellular protein transport
    • Shan, S.-O., ATPase and GTPase tangos drive intracellular protein transport. Trends Biochem. Sci. 41 (2016), 1050–1060.
    • (2016) Trends Biochem. Sci. , vol.41 , pp. 1050-1060
    • Shan, S.-O.1
  • 38
    • 33745307617 scopus 로고    scopus 로고
    • Ras, PI(3)K and mTOR signalling controls tumour cell growth
    • Shaw, R.J., Cantley, L.C., Ras, PI(3)K and mTOR signalling controls tumour cell growth. Nature 441 (2006), 424–430.
    • (2006) Nature , vol.441 , pp. 424-430
    • Shaw, R.J.1    Cantley, L.C.2
  • 39
    • 0029831063 scopus 로고    scopus 로고
    • Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions
    • Simon, I., Zerial, M., Goody, R.S., Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions. J. Biol. Chem. 271 (1996), 20470–20478.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20470-20478
    • Simon, I.1    Zerial, M.2    Goody, R.S.3
  • 41
    • 0029905455 scopus 로고    scopus 로고
    • A GTPase distinct from Ran is involved in nuclear protein import
    • Sweet, D.J., Gerace, L., A GTPase distinct from Ran is involved in nuclear protein import. J. Cell Biol. 133 (1996), 971–983.
    • (1996) J. Cell Biol. , vol.133 , pp. 971-983
    • Sweet, D.J.1    Gerace, L.2
  • 42
    • 84888200442 scopus 로고    scopus 로고
    • The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1
    • Tsun, Z.-Y., Bar-Peled, L., Chantranupong, L., Zoncu, R., Wang, T., Kim, C., Spooner, E., Sabatini, D.M., The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1. Mol. Cell 52 (2013), 495–505.
    • (2013) Mol. Cell , vol.52 , pp. 495-505
    • Tsun, Z.-Y.1    Bar-Peled, L.2    Chantranupong, L.3    Zoncu, R.4    Wang, T.5    Kim, C.6    Spooner, E.7    Sabatini, D.M.8
  • 43
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport
    • Vetter, I.R., Nowak, C., Nishimoto, T., Kuhlmann, J., Wittinghofer, A., Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature 398 (1999), 39–46.
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 44
    • 24644453120 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae GTPase complex: Gtr1p-Gtr2p regulates cell-proliferation through Saccharomyces cerevisiae Ran-binding protein, Yrb2p
    • Wang, Y., Nakashima, N., Sekiguchi, T., Nishimoto, T., Saccharomyces cerevisiae GTPase complex: Gtr1p-Gtr2p regulates cell-proliferation through Saccharomyces cerevisiae Ran-binding protein, Yrb2p. Biochem. Biophys. Res. Commun. 336 (2005), 639–645.
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 639-645
    • Wang, Y.1    Nakashima, N.2    Sekiguchi, T.3    Nishimoto, T.4
  • 46
    • 84879073039 scopus 로고    scopus 로고
    • A critical review of mTOR inhibitors and epilepsy: from basic science to clinical trials
    • Wong, M., A critical review of mTOR inhibitors and epilepsy: from basic science to clinical trials. Expert Rev. Neurother. 13 (2013), 657–669.
    • (2013) Expert Rev. Neurother. , vol.13 , pp. 657-669
    • Wong, M.1
  • 47
    • 0017697623 scopus 로고
    • Direct and specific photochemical cross-linking of adenosine 5′-triphosphate to an aminoacyl-tRNA synthetase
    • Yue, V.T., Schimmel, P.R., Direct and specific photochemical cross-linking of adenosine 5′-triphosphate to an aminoacyl-tRNA synthetase. Biochemistry 16 (1977), 4678–4684.
    • (1977) Biochemistry , vol.16 , pp. 4678-4684
    • Yue, V.T.1    Schimmel, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.