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Volumn 10, Issue 10, 2015, Pages 1767-1777

Dynamic Visualization of mTORC1 Activity in Living Cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; GROWTH FACTOR; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; PLATELET DERIVED GROWTH FACTOR; PROTEIN KINASE B;

EID: 84925136709     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2015.02.031     Document Type: Article
Times cited : (98)

References (61)
  • 3
    • 27244445187 scopus 로고    scopus 로고
    • Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity
    • Ananthanarayanan B., Ni Q., Zhang J. Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity. Proc. Natl. Acad. Sci. USA 2005, 102:15081-15086.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15081-15086
    • Ananthanarayanan, B.1    Ni, Q.2    Zhang, J.3
  • 4
    • 81855212711 scopus 로고    scopus 로고
    • The expanding relevance of nuclear mTOR in carcinogenesis
    • Back J.H., Kim A.L. The expanding relevance of nuclear mTOR in carcinogenesis. Cell Cycle 2011, 10:3849-3852.
    • (2011) Cell Cycle , vol.10 , pp. 3849-3852
    • Back, J.H.1    Kim, A.L.2
  • 5
    • 84866431363 scopus 로고    scopus 로고
    • Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1
    • Bar-Peled L., Schweitzer L.D., Zoncu R., Sabatini D.M. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell 2012, 150:1196-1208.
    • (2012) Cell , vol.150 , pp. 1196-1208
    • Bar-Peled, L.1    Schweitzer, L.D.2    Zoncu, R.3    Sabatini, D.M.4
  • 7
    • 84890149646 scopus 로고    scopus 로고
    • Where is mTOR and what is it doing there?
    • Betz C., Hall M.N. Where is mTOR and what is it doing there?. J.Cell Biol. 2013, 203:563-574.
    • (2013) J.Cell Biol. , vol.203 , pp. 563-574
    • Betz, C.1    Hall, M.N.2
  • 8
    • 33646143793 scopus 로고    scopus 로고
    • Localization of Rheb to the endomembrane is critical for its signaling function
    • 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.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 869-880
    • Buerger, C.1    DeVries, B.2    Stambolic, V.3
  • 11
    • 0030888163 scopus 로고    scopus 로고
    • The Ras-related protein Rheb is farnesylated and antagonizes Ras signaling and transformation
    • Clark G.J., Kinch M.S., Rogers-Graham K., Sebti S.M., Hamilton A.D., Der C.J. The Ras-related protein Rheb is farnesylated and antagonizes Ras signaling and transformation. J.Biol. Chem. 1997, 272:10608-10615.
    • (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
  • 12
    • 84894212463 scopus 로고    scopus 로고
    • Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2
    • Demetriades C., Doumpas N., Teleman A.A. Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2. Cell 2014, 156:786-799.
    • (2014) Cell , vol.156 , pp. 786-799
    • Demetriades, C.1    Doumpas, N.2    Teleman, A.A.3
  • 13
    • 78650157273 scopus 로고    scopus 로고
    • Visualization of PKA activity in plasma membrane microdomains
    • Depry C., Allen M.D., Zhang J. Visualization of PKA activity in plasma membrane microdomains. Mol. Biosyst. 2011, 7:52-58.
    • (2011) Mol. Biosyst. , vol.7 , pp. 52-58
    • Depry, C.1    Allen, M.D.2    Zhang, J.3
  • 14
    • 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. 2013, 15:555-564.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 555-564
    • Dibble, C.C.1    Manning, B.D.2
  • 16
  • 17
    • 0030934285 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in the translational regulator, PHAS-I, that are controlled by insulin and rapamycin in rat adipocytes
    • Fadden P., Haystead T.A., Lawrence J.C. Identification of phosphorylation sites in the translational regulator, PHAS-I, that are controlled by insulin and rapamycin in rat adipocytes. J.Biol. Chem. 1997, 272:10240-10247.
    • (1997) J.Biol. Chem. , vol.272 , pp. 10240-10247
    • Fadden, P.1    Haystead, T.A.2    Lawrence, J.C.3
  • 18
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • Fang Y., Vilella-Bach M., Bachmann R., Flanigan A., Chen J. Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 2001, 294:1942-1945.
    • (2001) Science , vol.294 , pp. 1942-1945
    • Fang, Y.1    Vilella-Bach, M.2    Bachmann, R.3    Flanigan, A.4    Chen, J.5
  • 19
    • 84876559631 scopus 로고    scopus 로고
    • Platelet-derived growth factor-BB activates calcium/calmodulin-dependent and -independent mechanisms that mediate Akt phosphorylation in the neurofibromin-deficient human Schwann cell line ST88-14
    • Farrer R.G., Farrer J.R., DeVries G.H. Platelet-derived growth factor-BB activates calcium/calmodulin-dependent and -independent mechanisms that mediate Akt phosphorylation in the neurofibromin-deficient human Schwann cell line ST88-14. J.Biol. Chem. 2013, 288:11066-11073.
    • (2013) J.Biol. Chem. , vol.288 , pp. 11066-11073
    • Farrer, R.G.1    Farrer, J.R.2    DeVries, G.H.3
  • 20
    • 0031821410 scopus 로고    scopus 로고
    • The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein
    • Fletcher C.M., Wagner G. The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein. Protein Sci. 1998, 7:1639-1642.
    • (1998) Protein Sci. , vol.7 , pp. 1639-1642
    • Fletcher, C.M.1    Wagner, G.2
  • 21
    • 57349145336 scopus 로고    scopus 로고
    • Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains
    • Gao X., Zhang J. Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains. Mol. Biol. Cell 2008, 19:4366-4373.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4366-4373
    • Gao, X.1    Zhang, J.2
  • 22
    • 84869005068 scopus 로고    scopus 로고
    • Withdrawal of essential amino acids increases autophagy by a pathway involving Ca2+/calmodulin-dependent kinase-β (CaMKK-β)
    • Ghislat G., Patron M., Rizzuto R., Knecht E. Withdrawal of essential amino acids increases autophagy by a pathway involving Ca2+/calmodulin-dependent kinase-β (CaMKK-β). J.Biol. Chem. 2012, 287:38625-38636.
    • (2012) J.Biol. Chem. , vol.287 , pp. 38625-38636
    • Ghislat, G.1    Patron, M.2    Rizzuto, R.3    Knecht, E.4
  • 24
  • 26
    • 34248195469 scopus 로고    scopus 로고
    • Lipid rafts and membrane traffic
    • Hanzal-Bayer M.F., Hancock J.F. Lipid rafts and membrane traffic. FEBS Lett. 2007, 581:2098-2104.
    • (2007) FEBS Lett. , vol.581 , pp. 2098-2104
    • Hanzal-Bayer, M.F.1    Hancock, J.F.2
  • 27
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • Hara K., Yonezawa K., Weng Q.P., Kozlowski M.T., Belham C., Avruch J. Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J.Biol. Chem. 1998, 273:14484-14494.
    • (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
  • 28
    • 0032533173 scopus 로고    scopus 로고
    • Insulin-stimulated kinase from rat fat cells that phosphorylates initiation factor 4E-binding protein 1 on the rapamycin-insensitive site (serine-111)
    • Heesom K.J., Avison M.B., Diggle T.A., Denton R.M. Insulin-stimulated kinase from rat fat cells that phosphorylates initiation factor 4E-binding protein 1 on the rapamycin-insensitive site (serine-111). Biochem. J. 1998, 336:39-48.
    • (1998) Biochem. J. , vol.336 , pp. 39-48
    • Heesom, K.J.1    Avison, M.B.2    Diggle, T.A.3    Denton, R.M.4
  • 30
    • 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., Su B. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell 2006, 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
  • 31
    • 84884676252 scopus 로고    scopus 로고
    • Nutrient signaling to mTOR and cell growth
    • Jewell J.L., Guan K.L. Nutrient signaling to mTOR and cell growth. Trends Biochem. Sci. 2013, 38:233-242.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 233-242
    • Jewell, J.L.1    Guan, K.L.2
  • 32
    • 77955287244 scopus 로고    scopus 로고
    • MTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1
    • Kantidakis T., Ramsbottom B.A., Birch J.L., Dowding S.N., White R.J. mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1. Proc. Natl. Acad. Sci. USA 2010, 107:11823-11828.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11823-11828
    • Kantidakis, T.1    Ramsbottom, B.A.2    Birch, J.L.3    Dowding, S.N.4    White, R.J.5
  • 34
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J., Kundu M., Viollet B., Guan K.L. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 2011, 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
  • 35
    • 70350418625 scopus 로고    scopus 로고
    • MTOR signaling at a glance
    • Laplante M., Sabatini D.M. mTOR signaling at a glance. J.Cell Sci. 2009, 122:3589-3594.
    • (2009) J.Cell Sci. , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 37
    • 84892853050 scopus 로고    scopus 로고
    • Ral and Rheb GTPase activating proteins integrate mTOR and GTPase signaling in aging, autophagy, and tumor cell invasion
    • Martin T.D., Chen X.W., Kaplan R.E., Saltiel A.R., Walker C.L., Reiner D.J., Der C.J. Ral and Rheb GTPase activating proteins integrate mTOR and GTPase signaling in aging, autophagy, and tumor cell invasion. Mol. Cell 2014, 53:209-220.
    • (2014) Mol. Cell , vol.53 , pp. 209-220
    • Martin, T.D.1    Chen, X.W.2    Kaplan, R.E.3    Saltiel, A.R.4    Walker, C.L.5    Reiner, D.J.6    Der, C.J.7
  • 38
    • 79959451416 scopus 로고    scopus 로고
    • Reporting from the field: genetically encoded fluorescent reporters uncover signaling dynamics in living biological systems
    • Mehta S., Zhang J. Reporting from the field: genetically encoded fluorescent reporters uncover signaling dynamics in living biological systems. Annu. Rev. Biochem. 2011, 80:375-401.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 375-401
    • Mehta, S.1    Zhang, J.2
  • 40
    • 84871901272 scopus 로고    scopus 로고
    • Novel role for SHP-2 innutrient-responsive control of S6 kinase 1 signaling
    • Mercan F., Lee H., Kolli S., Bennett A.M. Novel role for SHP-2 innutrient-responsive control of S6 kinase 1 signaling. Mol. Cell. Biol. 2013, 33:293-306.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 293-306
    • Mercan, F.1    Lee, H.2    Kolli, S.3    Bennett, A.M.4
  • 41
    • 33750345725 scopus 로고    scopus 로고
    • Analyzing protein kinase dynamics in living cells with FRET reporters
    • Ni Q., Titov D.V., Zhang J. Analyzing protein kinase dynamics in living cells with FRET reporters. Methods 2006, 40:279-286.
    • (2006) Methods , vol.40 , pp. 279-286
    • Ni, Q.1    Titov, D.V.2    Zhang, J.3
  • 43
    • 53149083731 scopus 로고    scopus 로고
    • Syndecan-4 regulates subcellular localization of mTOR Complex2 and Akt activation in a PKCalpha-dependent manner in endothelial cells
    • Partovian C., Ju R., Zhuang Z.W., Martin K.A., Simons M. Syndecan-4 regulates subcellular localization of mTOR Complex2 and Akt activation in a PKCalpha-dependent manner in endothelial cells. Mol. Cell 2008, 32:140-149.
    • (2008) Mol. Cell , vol.32 , pp. 140-149
    • Partovian, C.1    Ju, R.2    Zhuang, Z.W.3    Martin, K.A.4    Simons, M.5
  • 44
    • 84890303026 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced Akt phosphorylation requires mTOR/Rictor and phospholipase C-γ1, whereas S6 phosphorylation depends on mTOR/Raptor and phospholipase D
    • Razmara M., Heldin C.H., Lennartsson J. Platelet-derived growth factor-induced Akt phosphorylation requires mTOR/Rictor and phospholipase C-γ1, whereas S6 phosphorylation depends on mTOR/Raptor and phospholipase D. Cell Commun. Signal. 2013, 11:3.
    • (2013) Cell Commun. Signal. , vol.11 , pp. 3
    • Razmara, M.1    Heldin, C.H.2    Lennartsson, J.3
  • 45
    • 0018722585 scopus 로고
    • Accumulation of amino acids by lysosomes incubated with amino acid methyl esters
    • Reeves J.P. Accumulation of amino acids by lysosomes incubated with amino acid methyl esters. J.Biol. Chem. 1979, 254:8914-8921.
    • (1979) J.Biol. Chem. , vol.254 , pp. 8914-8921
    • Reeves, J.P.1
  • 46
    • 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
    • Rosner M., Hengstschläger 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.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2934-2948
    • Rosner, M.1    Hengstschläger, M.2
  • 47
    • 84555178353 scopus 로고    scopus 로고
    • Detection of cytoplasmic and nuclear functions of mTOR by fractionation
    • Rosner M., Hengstschläger M. Detection of cytoplasmic and nuclear functions of mTOR by fractionation. Methods Mol. Biol. 2012, 821:105-124.
    • (2012) Methods Mol. Biol. , vol.821 , pp. 105-124
    • Rosner, M.1    Hengstschläger, M.2
  • 48
    • 4544384577 scopus 로고    scopus 로고
    • Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
    • Roux P.P., Ballif B.A., Anjum R., Gygi S.P., Blenis J. Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc. Natl. Acad. Sci. USA 2004, 101:13489-13494.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13489-13494
    • Roux, P.P.1    Ballif, B.A.2    Anjum, R.3    Gygi, S.P.4    Blenis, J.5
  • 50
    • 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 2010, 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
  • 51
    • 25444450400 scopus 로고    scopus 로고
    • Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway
    • Takahashi K., Nakagawa M., Young S.G., 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.
    • (2005) J.Biol. Chem. , vol.280 , pp. 32768-32774
    • Takahashi, K.1    Nakagawa, M.2    Young, S.G.3    Yamanaka, S.4
  • 52
    • 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., Rosa J.L. Amino acids activate mammalian target of rapamycin complex 2 (mTORC2) via PI3K/Akt signaling. J.Biol. Chem. 2011, 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
  • 53
    • 0141733228 scopus 로고    scopus 로고
    • Inactivation of the tuberous sclerosis complex-1 and -2 gene products occurs by phosphoinositide 3-kinase/Akt-dependent and -independent phosphorylation of tuberin
    • Tee A.R., Anjum R., Blenis J. Inactivation of the tuberous sclerosis complex-1 and -2 gene products occurs by phosphoinositide 3-kinase/Akt-dependent and -independent phosphorylation of tuberin. J.Biol. Chem. 2003, 278:37288-37296.
    • (2003) J.Biol. Chem. , vol.278 , pp. 37288-37296
    • Tee, A.R.1    Anjum, R.2    Blenis, J.3
  • 55
    • 79953732149 scopus 로고    scopus 로고
    • A fluorescent reporter of AMPK activity and cellular energy stress
    • Tsou P., Zheng B., Hsu C.H., Sasaki A.T., Cantley L.C. A fluorescent reporter of AMPK activity and cellular energy stress. Cell Metab. 2011, 13:476-486.
    • (2011) Cell Metab. , vol.13 , pp. 476-486
    • Tsou, P.1    Zheng, B.2    Hsu, C.H.3    Sasaki, A.T.4    Cantley, L.C.5
  • 56
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • Violin J.D., Zhang J., Tsien R.Y., Newton A.C. A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. J.Cell Biol. 2003, 161:899-909.
    • (2003) J.Cell Biol. , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 57
    • 0029021621 scopus 로고
    • Identification of tuberin, the tuberous sclerosis-2 product. Tuberin possesses specific Rap1GAP activity
    • Wienecke R., König A., DeClue J.E. Identification of tuberin, the tuberous sclerosis-2 product. Tuberin possesses specific Rap1GAP activity. J.Biol. Chem. 1995, 270:16409-16414.
    • (1995) J.Biol. Chem. , vol.270 , pp. 16409-16414
    • Wienecke, R.1    König, A.2    DeClue, J.E.3
  • 58
    • 84897977386 scopus 로고    scopus 로고
    • Environmental signaling through the mechanistic target of rapamycin complex 1: mTORC1 goes nuclear
    • Workman J.J., Chen H., Laribee R.N. Environmental signaling through the mechanistic target of rapamycin complex 1: mTORC1 goes nuclear. Cell Cycle 2014, 13:714-725.
    • (2014) Cell Cycle , vol.13 , pp. 714-725
    • Workman, J.J.1    Chen, H.2    Laribee, R.N.3
  • 59
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • Zhang J., Ma Y., Taylor S.S., Tsien R.Y. Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc. Natl. Acad. Sci. USA 2001, 98:14997-15002.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14997-15002
    • Zhang, J.1    Ma, Y.2    Taylor, S.S.3    Tsien, R.Y.4
  • 60
    • 84862950678 scopus 로고    scopus 로고
    • Visualizing dynamic activities of signaling enzymes using genetically encodable FRET-based biosensors from designs to applications
    • Zhou X., Herbst-Robinson K.J., Zhang J. Visualizing dynamic activities of signaling enzymes using genetically encodable FRET-based biosensors from designs to applications. Methods Enzymol. 2012, 504:317-340.
    • (2012) Methods Enzymol. , vol.504 , pp. 317-340
    • Zhou, X.1    Herbst-Robinson, K.J.2    Zhang, J.3
  • 61
    • 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 D.M. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 2011, 334:678-683.
    • (2011) Science , 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


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