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Volumn 287, Issue 31, 2012, Pages 26409-26422

Epidermal growth factor-induced vacuolar (H+)-ATPase assembly: A role in signaling via mTORC1 activation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBIOTICS; BIOSYNTHESIS; ENZYMES; PHOSPHORYLATION; PROTEOMICS; RATS;

EID: 84864388778     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.352229     Document Type: Article
Times cited : (45)

References (85)
  • 1
    • 0023023424 scopus 로고
    • Epidermal growth factor receptor kinase translocation and activation in vivo
    • Kay, D. G., Lai, W. H., Uchihashi, M., Khan, M. N., Posner, B. I., and Bergeron, J. J. (1986) Epidermal growth factor receptor kinase translocation and activation in vivo. J. Biol. Chem. 261, 8473-8480
    • (1986) J. Biol. Chem. , vol.261 , pp. 8473-8480
    • Kay, D.G.1    Lai, W.H.2    Uchihashi, M.3    Khan, M.N.4    Posner, B.I.5    Bergeron, J.J.6
  • 2
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • DOI 10.1038/nrm1360
    • Gruenberg, J., and Stenmark, H. (2004) The biogenesis of multivesicular endosomes. Nat. Rev. Mol. Cell Biol. 5, 317-323 (Pubitemid 38480612)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.4 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 3
    • 0024807218 scopus 로고
    • Ligand-mediated internalization, recycling, and downregulation of the epidermal growth factor receptor in vivo
    • DOI 10.1083/jcb.109.6.2741
    • Lai, W. H., Cameron, P. H., Wada, I., Doherty, J. J., 2nd, Kay, D. G., Posner, B. I., and Bergeron, J. J. (1989) Ligand-mediated internalization, recycling, and down-regulation of the epidermal growth factor receptor in vivo. J. Cell Biol. 109, 2741-2749 (Pubitemid 20011901)
    • (1989) Journal of Cell Biology , vol.109 , Issue.6 I , pp. 2741-2749
    • Lai, W.H.1    Cameron, P.H.2    Wada, I.3    Doherty II, J.-J.4    Kay, D.G.5    Posner, B.I.6    Bergeron, J.J.M.7
  • 4
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • Di Guglielmo, G. M., Baass, P. C., Ou, W. J., Posner, B. I., and Bergeron, J. J. (1994) Compartmentalization of SHC, GRB2, and mSOS and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 13, 4269-4277 (Pubitemid 24295199)
    • (1994) EMBO Journal , vol.13 , Issue.18 , pp. 4269-4277
    • Di, G.G.M.1    Baass, P.C.2    Ou, W.-J.3    Posner, B.I.4    Bergeron, J.J.M.5
  • 5
    • 0022997598 scopus 로고
    • Characterization of rat liver endosomal fractions. In vivo activation of insulin-stimulable receptor kinase in these structures
    • Khan, M. N., Savoie, S., Bergeron, J. J., and Posner, B. I. (1986) Characterization of rat liver endosomal fractions. In vivo activation of insulin-stimulable receptor kinase in these structures. J. Biol. Chem. 261, 8462-8472 (Pubitemid 17202727)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.18 , pp. 8462-8472
    • Khan, M.N.1    Savoie, S.2    Bergeron, J.J.M.3    Posner, B.I.4
  • 6
    • 0033696873 scopus 로고    scopus 로고
    • Compartmentalization and insulin-induced translocations of insulin receptor substrates, phosphatidylinositol 3-kinase, and protein kinase B in rat liver
    • Balbis, A., Baquiran, G., Bergeron, J. J., and Posner, B. I. (2000) Compartmentalization and insulin-induced translocations of insulin receptor substrates, phosphatidylinositol 3-kinase, and protein kinase B in rat liver. Endocrinology 141, 4041-4049
    • (2000) Endocrinology , vol.141 , pp. 4041-4049
    • Balbis, A.1    Baquiran, G.2    Bergeron, J.J.3    Posner, B.I.4
  • 7
    • 0036787904 scopus 로고    scopus 로고
    • Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival
    • Wang, Y., Pennock, S., Chen, X., and Wang, Z. (2002) Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival. Mol. Cell. Biol. 22, 7279-7290
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7279-7290
    • Wang, Y.1    Pennock, S.2    Chen, X.3    Wang, Z.4
  • 8
    • 0028952140 scopus 로고
    • Selective activation of the rat hepatic endosomal insulin receptor kinase. Role for the endosome in insulin signaling
    • Bevan, A. P., Burgess, J. W., Drake, P. G., Shaver, A., Bergeron, J. J., and Posner, B. I. (1995) Selective activation of the rat hepatic endosomal insulin receptor kinase. Role for the endosome in insulin signaling. J. Biol. Chem. 270, 10784-10791
    • (1995) J. Biol. Chem. , vol.270 , pp. 10784-10791
    • Bevan, A.P.1    Burgess, J.W.2    Drake, P.G.3    Shaver, A.4    Bergeron, J.J.5    Posner, B.I.6
  • 9
    • 3142592401 scopus 로고    scopus 로고
    • Not just a sink: Endosomes in control of signal transduction
    • DOI 10.1016/j.ceb.2004.06.005, PII S0955067404000742
    • Miaczynska, M., Pelkmans, L., and Zerial, M. (2004) Not just a sink. Endosomes in control of signal transduction. Curr. Opin. Cell Biol. 16, 400-406 (Pubitemid 38903146)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 400-406
    • Miaczynska, M.1    Pelkmans, L.2    Zerial, M.3
  • 11
  • 12
    • 4544366537 scopus 로고    scopus 로고
    • Effect of insulin on caveolin-enriched membrane domains in rat liver
    • DOI 10.1074/jbc.M404280200
    • Balbis, A., Baquiran, G., Mounier, C., and Posner, B. I. (2004) Effect of insulin on caveolin-enriched membrane domains in rat liver. J. Biol. Chem. 279, 39348-39357 (Pubitemid 39258197)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39348-39357
    • Balbis, A.1    Baquiran, G.2    Mounier, C.3    Posner, B.I.4
  • 13
    • 0037924355 scopus 로고    scopus 로고
    • 1 binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: Roles in endoplasmic reticulum lipid compartmentalization and export
    • DOI 10.1124/jpet.103.051284
    • Hayashi, T., and Su, T. P. (2003) δ1 Receptors (δ1 binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum. Roles in endoplasmic reticulum lipid compartmentalization and export. J. Pharmacol. Exp. Ther. 306, 718-725 (Pubitemid 36886173)
    • (2003) Journal of Pharmacology and Experimental Therapeutics , vol.306 , Issue.2 , pp. 718-725
    • Hayashi, T.1    Su, T.-P.2
  • 14
    • 33645224087 scopus 로고    scopus 로고
    • Lipid and peptide control of phosphatidylinositol 4-kinase IIα activity on Golgi-endosomal rafts
    • DOI 10.1074/jbc.M506527200
    • Waugh, M. G., Minogue, S., Chotai, D., Berditchevski, F., and Hsuan, J. J. (2006) Lipid and peptide control of phosphatidylinositol 4-kinase IIα activity on Golgi-endosomal rafts. J. Biol. Chem. 281, 3757-3763 (Pubitemid 43847799)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 3757-3763
    • Waugh, M.G.1    Minogue, S.2    Chotai, D.3    Berditchevski, F.4    Hsuan, J.J.5
  • 15
    • 34250873547 scopus 로고    scopus 로고
    • Compartmentalization of signaling-competent epidermal growth factor receptors in endosomes
    • DOI 10.1210/en.2006-1674
    • Balbis, A., Parmar, A., Wang, Y., Baquiran, G., and Posner, B. I. (2007) Compartmentalization of signaling-competent epidermal growth factor receptors in endosomes. Endocrinology 148, 2944-2954 (Pubitemid 46984805)
    • (2007) Endocrinology , vol.148 , Issue.6 , pp. 2944-2954
    • Balbis, A.1    Parmar, A.2    Wang, Y.3    Baquiran, G.4    Posner, B.I.5
  • 16
    • 0034988887 scopus 로고    scopus 로고
    • Depletion of rafts in late endocytic membranes is controlled by NPC1-dependent recycling of cholesterol to the plasma membrane
    • Lusa, S., Blom, T. S., Eskelinen, E. L., Kuismanen, E., Månsson, J. E., Simons, K., and Ikonen, E. (2001) Depletion of rafts in late endocytic membranes is controlled by NPC1-dependent recycling of cholesterol to the plasma membrane. J. Cell Sci. 114, 1893-1900
    • (2001) J. Cell Sci. , vol.114 , pp. 1893-1900
    • Lusa, S.1    Blom, T.S.2    Eskelinen, E.L.3    Kuismanen, E.4    Månsson, J.E.5    Simons, K.6    Ikonen, E.7
  • 17
    • 66149171646 scopus 로고    scopus 로고
    • Compartmentalization of epidermal growth factor receptor in liver plasma membrane
    • Wang, Y., Posner, B. I., and Balbis, A. (2009) Compartmentalization of epidermal growth factor receptor in liver plasma membrane. J. Cell. Biochem. 107, 96-103
    • (2009) J. Cell. Biochem. , vol.107 , pp. 96-103
    • Wang, Y.1    Posner, B.I.2    Balbis, A.3
  • 18
    • 70349305428 scopus 로고    scopus 로고
    • Epidermal growth factor receptor signaling in liver cell proliferation and apoptosis
    • Reinehr, R., and Häussinger, D. (2009) Epidermal growth factor receptor signaling in liver cell proliferation and apoptosis. Biol. Chem. 390, 1033-1037
    • (2009) Biol. Chem. , vol.390 , pp. 1033-1037
    • Reinehr, R.1    Häussinger, D.2
  • 20
    • 0033305388 scopus 로고    scopus 로고
    • Epidermal growth factor and insulin-induced deoxyribonucleic acid synthesis in primary rat hepatocytes is phosphatidylinositol 3-kinase dependent and dissociated from protooncogene induction
    • Band, C. J., Mounier, C., and Posner, B. I. (1999) Epidermal growth factor and insulin-induced deoxyribonucleic acid synthesis in primary rat hepatocytes is phosphatidylinositol 3-kinase dependent and dissociated from protooncogene induction. Endocrinology 140, 5626-5634 (Pubitemid 30645350)
    • (1999) Endocrinology , vol.140 , Issue.12 , pp. 5626-5634
    • Band, C.J.1    Mounier, C.2    Posner, B.I.3
  • 21
    • 0036830564 scopus 로고    scopus 로고
    • PI3K-FRAP/mTOR pathway is critical for hepatocyte proliferation whereas MEK/ERK supports both proliferation and survival
    • DOI 10.1053/jhep.2002.36160
    • Coutant, A., Rescan, C., Gilot, D., Loyer, P., Guguen-Guillouzo, C., and Baffet, G. (2002) PI3K-FRAP/mTOR pathway is critical for hepatocyte proliferation, whereas MEK/ERK supports both proliferation and survival. Hepatology 36, 1079-1088 (Pubitemid 35253423)
    • (2002) Hepatology , vol.36 , Issue.5 II , pp. 1079-1088
    • Coutant, A.1    Rescan, C.2    Gilot, D.3    Loyer, P.4    Guguen-Guillouzo, C.5    Baffet, G.6
  • 22
    • 33645158483 scopus 로고    scopus 로고
    • V-ATPase. A potential pH sensor
    • Recchi, C., and Chavrier, P. (2006) V-ATPase. A potential pH sensor. Nat. Cell Biol. 8, 107-109
    • (2006) Nat. Cell Biol. , vol.8 , pp. 107-109
    • Recchi, C.1    Chavrier, P.2
  • 23
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases. Nature's most versatile proton pumps
    • Nishi, T., and Forgac, M. (2002) The vacuolar (H+)-ATPases. Nature's most versatile proton pumps. Nat. Rev. Mol. Cell Biol. 3, 94-103
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 25
    • 47349120492 scopus 로고    scopus 로고
    • +-ATPase in vesicular trafficking. Targeting, regulation, and function
    • +-ATPase in vesicular trafficking. Targeting, regulation, and function. Curr. Opin. Cell Biol. 20, 415-426
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 26
    • 0029063512 scopus 로고
    • +- ATPase in vivo
    • +- ATPase in vivo. J. Biol. Chem. 270, 17025-17032
    • (1995) J. Biol. Chem. , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 27
    • 0031597366 scopus 로고    scopus 로고
    • +-ATPase is an unconventional glucose-induced effect
    • +-ATPase is an unconventional glucose-induced effect. Mol. Cell. Biol. 18, 7064-7074
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 28
    • 11844260070 scopus 로고    scopus 로고
    • +-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells
    • +-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells. Mol. Cell. Biol. 25, 575-589
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 575-589
    • Sautin, Y.Y.1    Lu, M.2    Gaugler, A.3    Zhang, L.4    Gluck, S.L.5
  • 29
    • 0018184182 scopus 로고
    • Isolation of rat liver lysosomes by isopycnic centrifugation in a metrizamide gradient
    • Wattiaux, R., Wattiaux-De Coninck, S., Ronveaux-dupal, M. F., and Dubois, F. (1978) Isolation of rat liver lysosomes by isopycnic centrifugation in a metrizamide gradient. J. Cell Biol. 78, 349-368 (Pubitemid 8403877)
    • (1978) Journal of Cell Biology , vol.78 , Issue.2 , pp. 349-368
    • Wattiaux, R.1    Wattiaux-De, C.S.2    Ronveaux-Dupal, M.F.3    Dubois, F.4
  • 30
    • 0034680848 scopus 로고    scopus 로고
    • Epidermal growth factor-induced phosphatidylinositol 3-kinase activation andDNAsynthesis. Identification of Grb2-associated binder 2 as the major mediator in rat hepatocytes
    • Kong, M., Mounier, C., Wu, J., and Posner, B. I. (2000) Epidermal growth factor-induced phosphatidylinositol 3-kinase activation andDNAsynthesis. Identification of Grb2-associated binder 2 as the major mediator in rat hepatocytes. J. Biol. Chem. 275, 36035-36042
    • (2000) J. Biol. Chem. , vol.275 , pp. 36035-36042
    • Kong, M.1    Mounier, C.2    Wu, J.3    Posner, B.I.4
  • 32
    • 0018822124 scopus 로고
    • Radioiodination of proteins by the use of the chloramine-T method
    • McConahey, P. J., and Dixon, F. J. (1980) Radioiodination of proteins by the use of the chloramine-T method. Methods Enzymol. 70, 210-213
    • (1980) Methods Enzymol. , vol.70 , pp. 210-213
    • McConahey, P.J.1    Dixon, F.J.2
  • 34
    • 0037662713 scopus 로고    scopus 로고
    • Regulation of targets of mTOR (mammalian target of rapamycin) signalling by intracellular amino acid availability
    • DOI 10.1042/BJ20021266
    • Beugnet, A., Tee, A. R., Taylor, P. M., and Proud, C. G. (2003) Regulation of targets of mTOR (mammalian target of rapamycin) signaling by intracellular amino acid availability. Biochem. J. 372, 555-566 (Pubitemid 36723901)
    • (2003) Biochemical Journal , vol.372 , Issue.2 , pp. 555-566
    • Beugnet, A.1    Tee, A.R.2    Taylor, P.M.3    Proud, C.G.4
  • 35
    • 0026725764 scopus 로고
    • The dephosphorylation of insulin and epidermal growth factor receptors. Role of endosome-associated phosphotyrosine phosphatase(s)
    • Faure, R., Baquiran, G., Bergeron, J. J., and Posner, B. I. (1992) The dephosphorylation of insulin and epidermal growth factor receptors. Role of endosome-associated phosphotyrosine phosphatase(s). J. Biol. Chem. 267, 11215-11221
    • (1992) J. Biol. Chem. , vol.267 , pp. 11215-11221
    • Faure, R.1    Baquiran, G.2    Bergeron, J.J.3    Posner, B.I.4
  • 36
    • 0037458542 scopus 로고    scopus 로고
    • Epidermal growth factor-induced DNA synthesis: Key role for Src phosphorylation of the docking protein Gab2
    • DOI 10.1074/jbc.M208286200
    • Kong, M., Mounier, C., Dumas, V., and Posner, B. I. (2003) Epidermal growth factor-induced DNA synthesis. Key role for Src phosphorylation of the docking protein Gab2. J. Biol. Chem. 278, 5837-5844 (Pubitemid 36800830)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 5837-5844
    • Kong, M.1    Mounier, C.2    Dumas, V.3    Posner, B.I.4
  • 37
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins
    • DOI 10.1146/annurev.cellbio.19.110701.154617
    • Hicke, L., and Dunn, R. (2003) Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19, 141-172 (Pubitemid 37487346)
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 39
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases. Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007) Vacuolar ATPases. Rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 40
    • 0019792936 scopus 로고
    • Intracellular hormone receptors. Evidence for insulin and lactogen receptors in a unique vesicle sedimenting in lysosome fractions of rat liver
    • Khan, M. N., Posner, B. I., Verma, A. K., Khan, R. J., and Bergeron, J. J. (1981) Intracellular hormone receptors. Evidence for insulin and lactogen receptors in a unique vesicle sedimenting in lysosome fractions of rat liver. Proc. Natl. Acad. Sci. 78, 4980-4984
    • (1981) Proc. Natl. Acad. Sci. , vol.78 , pp. 4980-4984
    • Khan, M.N.1    Posner, B.I.2    Verma, A.K.3    Khan, R.J.4    Bergeron, J.J.5
  • 41
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases
    • Dröse, S., and Altendorf, K. (1997) Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J. Exp. Biol. 200, 1-8 (Pubitemid 27058890)
    • (1997) Journal of Experimental Biology , vol.200 , Issue.1 , pp. 1-8
    • Drose, S.1    Altendorf, K.2
  • 42
    • 33751085062 scopus 로고    scopus 로고
    • A model for the proteolipid ring and bafilomycin/concanamycin-binding site in the vacuolar ATPase of Neurospora crassa
    • DOI 10.1074/jbc.M605532200
    • Bowman, B. J., McCall, M. E., Baertsch, R., and Bowman, E. J. (2006) A model for the proteolipid ring and bafilomycin/concanamycin binding site in the vacuolar ATPase of Neurospora crassa. J. Biol. Chem. 281, 31885-31893 (Pubitemid 46041451)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31885-31893
    • Bowman, B.J.1    McCall, M.E.2    Baertsch, R.3    Bowman, E.J.4
  • 43
    • 28844433952 scopus 로고    scopus 로고
    • Subunit a of the yeast V-ATPase participates in binding of bafilomycin
    • DOI 10.1074/jbc.M509106200
    • Wang, Y., Inoue, T., and Forgac, M. (2005) Subunit a of the yeast VATPase participates in binding of bafilomycin. J. Biol. Chem. 280, 40481-40488 (Pubitemid 41780535)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40481-40488
    • Wang, Y.1    Inoue, T.2    Forgac, M.3
  • 44
    • 1842424890 scopus 로고    scopus 로고
    • Effect of Inhibiting Vacuolar Acidification on Insulin Signaling in Hepatocytes
    • DOI 10.1074/jbc.M311493200
    • Balbis, A., Baquiran, G., Dumas, V., and Posner, B. I. (2004) Effect of inhibiting vacuolar acidification on insulin signaling in hepatocytes. J. Biol. Chem. 279, 12777-12785 (Pubitemid 38445850)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12777-12785
    • Balbis, A.1    Baquiran, G.2    Dumas, V.3    Posner, B.I.4
  • 45
    • 0030022242 scopus 로고    scopus 로고
    • 1 in Swiss 3T3 fibroblasts
    • Saurin, A. J., Hamlett, J., Clague, M. J., and Pennington, S. R. (1996) Inhibition of mitogen-inducedDNAsynthesis by bafilomycin A1 in Swiss 3T3 fibroblasts. Biochem. J. 313, 65-70 (Pubitemid 26013426)
    • (1996) Biochemical Journal , vol.313 , Issue.1 , pp. 65-70
    • Saurin, A.J.1    Hamlett, J.2    Clague, M.J.3    Pennington, S.R.4
  • 47
    • 33751072389 scopus 로고    scopus 로고
    • Bafilomycin induces the p21-mediated growth inhibition of cancer cells under hypoxic conditions by expressing hypoxia-inducible factor-1α
    • DOI 10.1124/mol.106.028076
    • Lim, J. H., Park, J. W., Kim, M. S., Park, S. K., Johnson, R. S., and Chun, Y. S. (2006) Bafilomycin induces the p21-mediated growth inhibition of cancer cells under hypoxic conditions by expressing hypoxia-inducible factor-1α. Mol. Pharmacol. 70, 1856-1865 (Pubitemid 44771901)
    • (2006) Molecular Pharmacology , vol.70 , Issue.6 , pp. 1856-1865
    • Lim, J.-H.1    Park, J.-W.2    Kim, M.-S.3    Park, S.-K.4    Johnson, R.S.5    Chun, Y.-S.6
  • 48
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • DOI 10.1101/gad.1212704
    • Hay, N., and Sonenberg, N. (2004) Upstream and downstream of mTOR. Genes Dev. 18, 1926-1945 (Pubitemid 39071573)
    • (2004) Genes and Development , vol.18 , Issue.16 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 49
    • 0029876268 scopus 로고    scopus 로고
    • A vacuolar-type proton ATPase mediates acidification of plasmalemmal vesicles during potocytosis
    • DOI 10.1006/excr.1996.0133
    • Mineo, C., and Anderson, R. G. (1996) A vacuolar-type proton ATPase mediates acidification of plasmalemmal vesicles during potocytosis. Exp. Cell Res. 224, 237-242 (Pubitemid 26140557)
    • (1996) Experimental Cell Research , vol.224 , Issue.2 , pp. 237-242
    • Mineo, C.1    Anderson, R.G.W.2
  • 50
    • 0035798097 scopus 로고    scopus 로고
    • Mammalian TOR: A homeostatic ATP sensor
    • DOI 10.1126/science.1063518
    • Dennis, P. B., Jaeschke, A., Saitoh, M., Fowler, B., Kozma, S. C., and Thomas, G. (2001) Mammalian TOR. A homeostatic ATP sensor. Science 294, 1102-1105 (Pubitemid 33041865)
    • (2001) Science , vol.294 , Issue.5544 , pp. 1102-1105
    • Dennis, P.B.1    Jaeschke, A.2    Saitoh, M.3    Fowler, B.4    Kozma, S.C.5    Thomas, G.6
  • 51
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • DOI 10.1146/annurev.biochem.67.1.821
    • Hardie, D. G., Carling, D., and Carlson, M. (1998) The AMP-activated/SNF1 protein kinase subfamily. Metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67, 821-855 (Pubitemid 28411146)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 52
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
    • DOI 10.1016/S0092-8674(03)00929-2
    • Inoki, K., Zhu, T., and Guan, K. L. (2003) TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590 (Pubitemid 37506046)
    • (2003) Cell , vol.115 , Issue.5 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.-L.3
  • 53
    • 15044358594 scopus 로고    scopus 로고
    • New roles for the LKB1 3 AMPK pathway
    • Hardie, D. G. (2005) New roles for the LKB1 3 AMPK pathway. Curr. Opin. Cell Biol. 17, 167-173
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 167-173
    • Hardie, D.G.1
  • 54
    • 0043210478 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis
    • DOI 10.1074/jbc.M303946200
    • Woods, A., Vertommen, D., Neumann, D., Turk, R., Bayliss, J., Schlattner, U., Wallimann, T., Carling, D., and Rider, M. H. (2003) Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis. J. Biol. Chem. 278, 28434-28442 (Pubitemid 36935745)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28434-28442
    • Woods, A.1    Vertommen, D.2    Neumann, D.3    Turk, R.4    Bayliss, J.5    Schlattner, U.6    Wallimannll, T.7    Carling, D.8    Rider, M.H.9
  • 55
    • 70449397351 scopus 로고    scopus 로고
    • PRAS40. Target or modulator of mTORC1 signaling and insulin action?
    • Nascimento, E. B., and Ouwens, D. M. (2009) PRAS40. Target or modulator of mTORC1 signaling and insulin action? Arch. Physiol. Biochem. 115, 163-175
    • (2009) Arch. Physiol. Biochem. , vol.115 , pp. 163-175
    • Nascimento, E.B.1    Ouwens, D.M.2
  • 57
    • 34548359244 scopus 로고    scopus 로고
    • PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex
    • DOI 10.1074/jbc.M704406200
    • Fonseca, B. D., Smith, E. M., Lee, V. H., MacKintosh, C., and Proud, C. G. (2007) PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex. J. Biol. Chem. 282, 24514-24524 (Pubitemid 47347551)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24514-24524
    • Fonseca, B.D.1    Smith, E.M.2    Lee, V.H.-Y.3    MacKintosh, C.4    Proud, C.G.5
  • 60
    • 0037134492 scopus 로고    scopus 로고
    • Insulin promotes the cell surface recruitment of the SAT2/ATA2 system A amino acid transporter from an endosomal compartment in skeletal muscle cells
    • DOI 10.1074/jbc.M108609200
    • Hyde, R., Peyrollier, K., and Hundal, H. S. (2002) Insulin promotes the cell surface recruitment of the SAT2/ATA2 system A amino acid transporter from an endosomal compartment in skeletal muscle cells. J. Biol. Chem. 277, 13628-13634 (Pubitemid 34967962)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13628-13634
    • Hyde, R.1    Peyrollier, K.2    Hundal, H.S.3
  • 61
    • 21744459535 scopus 로고    scopus 로고
    • Regulation of mTOR and cell growth in response to energy stress by REDD1
    • DOI 10.1128/MCB.25.14.5834-5845.2005
    • Sofer, A., Lei, K., Johannessen, C. M., and Ellisen, L. W. (2005) Regulation of mTOR and cell growth in response to energy stress by REDD1. Mol. Cell. Biol. 25, 5834-5845 (Pubitemid 40946541)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.14 , pp. 5834-5845
    • Sofer, A.1    Lei, K.2    Johannessen, C.M.3    Ellisen, L.W.4
  • 62
    • 41249094257 scopus 로고    scopus 로고
    • Rapid turnover of the mTOR complex 1 (mTORC1) repressor REDD1 and activation of mTORC1 signaling following inhibition of pro- Tein synthesis
    • Kimball, S. R., Do, A. N., Kutzler, L., Cavener, D. R., and Jefferson, L. S. (2008) Rapid turnover of the mTOR complex 1 (mTORC1) repressor REDD1 and activation of mTORC1 signaling following inhibition of pro- tein synthesis. J. Biol. Chem. 283, 3465-3475
    • (2008) J. Biol. Chem. , vol.283 , pp. 3465-3475
    • Kimball, S.R.1    Do, A.N.2    Kutzler, L.3    Cavener, D.R.4    Jefferson, L.S.5
  • 63
    • 18044381192 scopus 로고    scopus 로고
    • Rheb binds and regulates the mTOR kinase
    • DOI 10.1016/j.cub.2005.02.053
    • Long, X., Lin, Y., Ortiz-Vega, S., Yonezawa, K., and Avruch, J. (2005) Rheb binds and regulates the mTOR kinase. Curr. Biol. 15, 702-713 (Pubitemid 40599924)
    • (2005) Current Biology , vol.15 , Issue.8 , pp. 702-713
    • Long, X.1    Lin, Y.2    Ortiz-Vega, S.3    Yonezawa, K.4    Avruch, J.5
  • 64
    • 45849105156 scopus 로고    scopus 로고
    • The rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • DOI 10.1126/science.1157535
    • Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., and Sabatini, D. M. (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
  • 65
    • 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., and Sabatini, D. M. (2010) Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 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
  • 66
    • 34249706373 scopus 로고    scopus 로고
    • Identification of endosomal epidermal growth factor receptor signaling targets by functional organelle proteomics
    • DOI 10.1074/mcp.M600463-MCP200
    • Stasyk, T., Schiefermeier, N., Skvortsov, S., Zwierzina, H., Peränen, J., Bonn, G. K., and Huber, L. A. (2007) Identification of endosomal epidermal growth factor receptor signaling targets by functional organelle proteomics. Mol. Cell. Proteomics 6, 908-922 (Pubitemid 46831940)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.5 , pp. 908-922
    • Stasyk, T.1    Schiefermeier, N.2    Skvortsov, S.3    Zwierzina, H.4    Peranen, J.5    Bonn, G.K.6    Hubeer, L.A.7
  • 67
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner, J. P., Dow, J. A., Earley, F. G., Klein, U., Jäger, D., and Wieczorek, H. (1995) Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem. 270, 5649-5653
    • (1995) J. Biol. Chem. , vol.270 , pp. 5649-5653
    • Sumner, J.P.1    Dow, J.A.2    Earley, F.G.3    Klein, U.4    Jäger, D.5    Wieczorek, H.6
  • 68
    • 0034629251 scopus 로고    scopus 로고
    • Regulation of V-ATPases by reversible disassembly
    • Kane, P. M. (2000) Regulation of V-ATPases by reversible disassembly. FEBS Lett. 469, 137-141
    • (2000) FEBS Lett. , vol.469 , pp. 137-141
    • Kane, P.M.1
  • 69
    • 33644935227 scopus 로고    scopus 로고
    • The V-type H+ ATPase. Molecular structure and function, physiological roles, and regulation
    • Beyenbach, K. W., and Wieczorek, H. (2006) The V-type H+ ATPase. Molecular structure and function, physiological roles, and regulation. J. Exp. Biol. 209, 577-589
    • (2006) J. Exp. Biol. , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 70
    • 0015496390 scopus 로고
    • Lysosomes, pH, and the anti-malarial action of chloroquine
    • Homewood, C. A., Warhurst, D. C., Peters, W., and Baggaley, V. C. (1972) Lysosomes, pH, and the anti-malarial action of chloroquine. Nature 235, 50-52
    • (1972) Nature , vol.235 , pp. 50-52
    • Homewood, C.A.1    Warhurst, D.C.2    Peters, W.3    Baggaley, V.C.4
  • 71
    • 69049097269 scopus 로고    scopus 로고
    • Tertiary active transport of amino acids reconstituted by coexpression of System A and L transporters in Xenopus oocytes
    • Baird, F. E., Bett, K. J., MacLean, C., Tee, A. R., Hundal, H. S., and Taylor, P. M. (2009) Tertiary active transport of amino acids reconstituted by coexpression of System A and L transporters in Xenopus oocytes. Am. J. Physiol. Endocrinol. Metab. 297, E822-E829
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.297
    • Baird, F.E.1    Bett, K.J.2    MacLean, C.3    Tee, A.R.4    Hundal, H.S.5    Taylor, P.M.6
  • 72
    • 65649152957 scopus 로고    scopus 로고
    • Amino acid transceptors. Gate keepers of nutrient exchange and regulators of nutrient signaling
    • Hundal, H. S., and Taylor, P. M. (2009) Amino acid transceptors. Gate keepers of nutrient exchange and regulators of nutrient signaling. Am. J. Physiol. Endocrinol. Metab. 296, E603-E613
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.296
    • Hundal, H.S.1    Taylor, P.M.2
  • 74
    • 0037155888 scopus 로고    scopus 로고
    • Intracellular sensing of amino acids in Xenopus laevis oocytes stimulates p70 S6 kinase in a target of rapamycin-dependent manner
    • DOI 10.1074/jbc.M107694200
    • Christie, G. R., Hajduch, E., Hundal, H. S., Proud, C. G., and Taylor, P. M. (2002) Intracellular sensing of amino acids in Xenopus laevis oocytes stimulates p70 S6 kinase in a target of rapamycin-dependent manner. J. Biol. Chem. 277, 9952-9957 (Pubitemid 34968102)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 9952-9957
    • Christie, G.R.1    Hajduch, E.2    Hundal, H.S.3    Proud, C.G.4    Taylor, P.M.5
  • 75
    • 0032508471 scopus 로고    scopus 로고
    • Effects of stress on amino acids and related compounds in various tissues of fasted rats
    • Dadmarz, M., vd Burg, C., Milakofsky, L., Hofford, J. M., and Vogel, W. H. (1998) Effects of stress on amino acids and related compounds in various tissues of fasted rats. Life Sci. 63, 1485-1491
    • (1998) Life Sci. , vol.63 , pp. 1485-1491
    • Dadmarz, M.1    Vd Burg, C.2    Milakofsky, L.3    Hofford, J.M.4    Vogel, W.H.5
  • 76
    • 0029916274 scopus 로고    scopus 로고
    • Effect of ethanol on amino acids and related compounds in rat plasma, heart, aorta, bronchus, and pancreas
    • DOI 10.1016/0741-8329(95)02031-4
    • Abdel-Nabi, R., Milakofsky, L., Hofford, J. M., Hare, T. A., and Vogel, W. H. (1996) Effect of ethanol on amino acids and related compounds in rat plasma, heart, aorta, bronchus, and pancreas. Alcohol 13, 171-174 (Pubitemid 26102098)
    • (1996) Alcohol , vol.13 , Issue.2 , pp. 171-174
    • Abdel-Nabi, R.1    Milakofsky, L.2    Hofford, J.M.3    Hare, T.A.4    Vogel, W.H.5
  • 77
    • 79961023008 scopus 로고    scopus 로고
    • EGF signaling activates the ubiquitin proteasome system to modulate C. elegans lifespan
    • Liu, G., Rogers, J., Murphy, C. T., and Rongo, C. (2011) EGF signaling activates the ubiquitin proteasome system to modulate C. elegans lifespan. EMBO J. 30, 2990-3003
    • (2011) EMBO J. , vol.30 , pp. 2990-3003
    • Liu, G.1    Rogers, J.2    Murphy, C.T.3    Rongo, C.4
  • 81
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an insideout mechanism that requires the vacuolar H-ATPase
    • Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., and Sabatini, D. M. (2011) mTORC1 senses lysosomal amino acids through an insideout mechanism that requires the vacuolar H-ATPase. Science 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
  • 82
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation
    • DOI 10.1074/jbc.M408278200
    • Shao, E., and Forgac, M. (2004) Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation. J. Biol. Chem. 279, 48663-48670 (Pubitemid 39625742)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 83
    • 0032486268 scopus 로고    scopus 로고
    • Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism
    • DOI 10.1074/jbc.273.23.14484
    • Hara, K., Yonezawa, K., Weng, Q. P., Kozlowski, M. T., Belham, C., and Avruch, J. (1998) Amino acid sufficiency and mTOR regulate p70 S6 kinase and eIF-4E BP1 through a common effector mechanism. J. Biol. Chem. 273, 14484-14494 (Pubitemid 28319170)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.23 , pp. 14484-14494
    • Hara, K.1    Yonezawa, K.2    Weng, Q.-P.3    Kozlowski, M.T.4    Belham, C.5    Avruch, J.6
  • 84
    • 0029907306 scopus 로고    scopus 로고
    • Growth hormone and the insulin-like growth factor system in myogenesis
    • DOI 10.1210/er.17.5.481
    • Florini, J. R., Ewton, D. Z., and Coolican, S. A. (1996) Growth hormone and the insulin-like growth factor system in myogenesis. Endocr. Rev. 17, 481-517 (Pubitemid 26346639)
    • (1996) Endocrine Reviews , vol.17 , Issue.5 , pp. 481-517
    • Florini, J.R.1    Ewton, D.Z.2    Coolican, S.A.3


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