메뉴 건너뛰기




Volumn 445, Issue , 2008, Pages 89-109

Amino acid regulation of autophagosome formation

Author keywords

AICAriboside (AICAR); Amino acid signaling; AMP activated protein kinase (AMPK); Beclin 1; Glutamate dehydrogenase; Insulin; Mammalian target of rapamycin (mTOR); Phosphatidylinositol 3 kinase (PI3 K); Reactive oxygen species.; Ribosomal protein S6

Indexed keywords

MAMMALIA;

EID: 84934444765     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-157-4_5     Document Type: Article
Times cited : (53)

References (115)
  • 1
    • 22044442015 scopus 로고    scopus 로고
    • Autophagosomes: Biogenesis from scratch?
    • Reggiori, F. and Klionsky, D. J. (2005) Autophagosomes: biogenesis from scratch? Curr. Opin. Cell Biol. 17, 415-422.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 415-422
    • Reggiori, F.1    Klionsky, D.J.2
  • 2
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • Yorimitsu, T. and Klionsky, D. J. (2005) Autophagy: molecular machinery for self-eating. Cell Death. Differ. 12, 1542-1552.
    • (2005) Cell Death. Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 3
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara, T., Nakamura, K., Matsui, M., et al. (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441, 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 4
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu, M., Waguri, S., Chiba,T., et al. (2006) Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441, 880-884.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3
  • 5
    • 0017697151 scopus 로고
    • Induction of autophagy by aminoacid deprivation in perfused rat liver
    • Mortimore, G. E. and Schworer, C. M. (1977) Induction of autophagy by aminoacid deprivation in perfused rat liver. Nature 270, 174-176.
    • (1977) Nature , vol.270 , pp. 174-176
    • Mortimore, G.E.1    Schworer, C.M.2
  • 6
    • 0030957959 scopus 로고    scopus 로고
    • Autophagic proteolysis: Control and specificity
    • Blommaart, E. F., Luiken, J. J., and Meijer, A. J. (1997) Autophagic proteolysis: control and specificity. Histochem. J. 29, 365-385.
    • (1997) Histochem. J , vol.29 , pp. 365-385
    • Blommaart, E.F.1    Luiken, J.J.2    Meijer, A.J.3
  • 7
    • 0014083718 scopus 로고
    • Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes
    • Deter, R. L. and De Duve, C. (1967) Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes. J. Cell Biol. 33, 437-449.
    • (1967) J. Cell Biol , vol.33 , pp. 437-449
    • Deter, R.L.1    De Duve, C.2
  • 9
    • 0038269032 scopus 로고    scopus 로고
    • Amino acids interfere with the ERK1/2-dependent control of macroautophagy by controlling the activation of Raf-1 in human colon cancer HT-29 cells
    • Pattingre, S., Bauvy, C., and Codogno, P. (2003) Amino acids interfere with the ERK1/2-dependent control of macroautophagy by controlling the activation of Raf-1 in human colon cancer HT-29 cells. J. Biol. Chem. 278, 16667-16674.
    • (2003) J. Biol. Chem , vol.278 , pp. 16667-16674
    • Pattingre, S.1    Bauvy, C.2    Codogno, P.3
  • 10
    • 33744783122 scopus 로고    scopus 로고
    • The hepatocyte integrin system and cell volume sensing
    • Häussinger, D., Reinehr, R., and Schliess, F. (2006) The hepatocyte integrin system and cell volume sensing. Acta Physiol (Oxf) 187, 249-255.
    • (2006) Acta Physiol (Oxf) , vol.187 , pp. 249-255
    • Häussinger, D.1    Reinehr, R.2    Schliess, F.3
  • 11
    • 0037312507 scopus 로고    scopus 로고
    • Tor signalling in bugs, brain and brawn
    • Jacinto, E. and Hall, M. N. (2003) Tor signalling in bugs, brain and brawn. Nat. Rev. Mol. Cell Biol. 4, 117-126.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 117-126
    • Jacinto, E.1    Hall, M.N.2
  • 12
    • 33645990907 scopus 로고    scopus 로고
    • Regulation of protein synthesis by insulin
    • Proud, C. G. (2006) Regulation of protein synthesis by insulin. Biochem. Soc. Trans. 34, 213-216.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 213-216
    • Proud, C.G.1
  • 13
    • 33645997012 scopus 로고    scopus 로고
    • Bridging the GAP between insulin signaling and GLUT4 translocation
    • Watson, R. T. and Pessin, J. E. (2006) Bridging the GAP between insulin signaling and GLUT4 translocation. Trends Biochem. Sci. 31, 215-222.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 215-222
    • Watson, R.T.1    Pessin, J.E.2
  • 14
    • 11244297916 scopus 로고    scopus 로고
    • Dysregulation of the TSCmTOR pathway in human disease
    • Inoki, K., Corradetti, M. N., and Guan, K. L. (2005) Dysregulation of the TSCmTOR pathway in human disease. Nat. Genet. 37, 19-24.
    • (2005) Nat. Genet , vol.37 , pp. 19-24
    • Inoki, K.1    Corradetti, M.N.2    Guan, K.L.3
  • 15
    • 33646548305 scopus 로고    scopus 로고
    • The amino acid sensitive TOR pathway from yeast to mammals
    • Dann, S. G. and Thomas, G. (2006) The amino acid sensitive TOR pathway from yeast to mammals. FEBS Lett. 580, 2821-2829.
    • (2006) FEBS Lett , vol.580 , pp. 2821-2829
    • Dann, S.G.1    Thomas, G.2
  • 16
    • 0027296748 scopus 로고
    • Inhibition of hepatocytic autophagy by okadaic acid and other protein phosphatase inhibitors
    • Holen, I., Gordon, P. B., and Seglen, P. O. (1993) Inhibition of hepatocytic autophagy by okadaic acid and other protein phosphatase inhibitors. Eur. J. Biochem. 215, 113-122.
    • (1993) Eur. J. Biochem , vol.215 , pp. 113-122
    • Holen, I.1    Gordon, P.B.2    Seglen, P.O.3
  • 17
    • 0028234322 scopus 로고
    • Cell swelling and the control of autophagic proteolysis in hepatocytes: Involvement of phosphorylation of ribosomal protein S6?
    • Luiken, J. J., Blommaart, E. F., Boon, L., van Woerkom, G. M., and Meijer, A. J. (1994) Cell swelling and the control of autophagic proteolysis in hepatocytes: involvement of phosphorylation of ribosomal protein S6? Biochem. Soc. Trans. 22, 508-511.
    • (1994) Biochem. Soc. Trans , vol.22 , pp. 508-511
    • Luiken, J.J.1    Blommaart, E.F.2    Boon, L.3    van Woerkom, G.M.4    Meijer, A.J.5
  • 18
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
    • Blommaart, E. F., Luiken, J. J., Blommaart, P. J., van Woerkom, G. M., and Meijer, A. J. (1995) Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J. Biol. Chem. 270, 2320-2326.
    • (1995) J. Biol. Chem , vol.270 , pp. 2320-2326
    • Blommaart, E.F.1    Luiken, J.J.2    Blommaart, P.J.3    van Woerkom, G.M.4    Meijer, A.J.5
  • 19
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • Shintani, T. and Klionsky, D. J. (2004) Autophagy in health and disease: a double-edged sword. Science 306, 990-995.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 20
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • Noda, T. and Ohsumi, Y. (1998) Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273, 3963-3966.
    • (1998) J. Biol. Chem , vol.273 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 21
    • 32944460806 scopus 로고    scopus 로고
    • In yeast, loss of Hogl leads to osmosensitivity of autophagy
    • Prick, T., Thumm, M., Kohrer, K., Häussinger, D., and vom Dahl, S. (2006) In yeast, loss of Hogl leads to osmosensitivity of autophagy. Biochem. J. 394, 153-161.
    • (2006) Biochem. J , vol.394 , pp. 153-161
    • Prick, T.1    Thumm, M.2    Kohrer, K.3    Häussinger, D.4    vom Dahl, S.5
  • 22
    • 11144219992 scopus 로고    scopus 로고
    • Glucagon represses signaling through the mammalian target of rapamycin in rat liver by activating AMP-activated protein kinase
    • Kimball, S. R., Siegfried, B. A., and Jefferson, L. S. (2004) Glucagon represses signaling through the mammalian target of rapamycin in rat liver by activating AMP-activated protein kinase. J. Biol. Chem. 279, 54103-54109.
    • (2004) J. Biol. Chem , vol.279 , pp. 54103-54109
    • Kimball, S.R.1    Siegfried, B.A.2    Jefferson, L.S.3
  • 23
    • 5644285347 scopus 로고    scopus 로고
    • In rat hepatocytes glucagon increases mammalian target of rapamycin phosphorylation on serine 2448 but antagonizes the phosphorylation of its downstream targets induced by insulin and amino acids
    • Mothe-Satney, I., Gautier, N., Hinault, C., Lawrence, J. C., Jr., and van Obberghen, E. (2004) In rat hepatocytes glucagon increases mammalian target of rapamycin phosphorylation on serine 2448 but antagonizes the phosphorylation of its downstream targets induced by insulin and amino acids. J. Biol. Chem. 279, 42628-42637.
    • (2004) J. Biol. Chem , vol.279 , pp. 42628-42637
    • Mothe-Satney, I.1    Gautier, N.2    Hinault, C.3    Lawrence Jr., J.C.4    van Obberghen, E.5
  • 24
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • Blommaart, E. F., Krause, U., Schellens, J. P., Vreeling-Sindelarova, H., and Meijer, A. J. (1997) The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes. Eur. J. Biochem. 243, 240-246.
    • (1997) Eur. J. Biochem , vol.243 , pp. 240-246
    • Blommaart, E.F.1    Krause, U.2    Schellens, J.P.3    Vreeling-Sindelarova, H.4    Meijer, A.J.5
  • 25
    • 0042326762 scopus 로고    scopus 로고
    • Muscarinic receptormediated activation of p70 S6 kinase 1 (S6K1) in 1321N1 astrocytoma cells: Permissive role of phosphoinositide 3-kinase
    • Tang, X., Wang, L., Proud, C. G., and Downes, C. P. (2003) Muscarinic receptormediated activation of p70 S6 kinase 1 (S6K1) in 1321N1 astrocytoma cells: permissive role of phosphoinositide 3-kinase. Biochem. J. 374, 137-143.
    • (2003) Biochem. J , vol.374 , pp. 137-143
    • Tang, X.1    Wang, L.2    Proud, C.G.3    Downes, C.P.4
  • 26
    • 26444575415 scopus 로고    scopus 로고
    • Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase
    • Nobukuni, T., Joaquin, M., Roccio, M., et al. (2005) Amino acids mediate mTOR/raptor signaling through activation of class 3 phosphatidylinositol 3OH-kinase. Proc. Natl. Acad. Sci. USA 102, 14238-14243.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14238-14243
    • Nobukuni, T.1    Joaquin, M.2    Roccio, M.3
  • 27
    • 25444457577 scopus 로고    scopus 로고
    • hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase
    • Byfield, M. P., Murray, J. T., and Backer, J. M. (2005) hVps34 is a nutrient-regulated lipid kinase required for activation of p70 S6 kinase. J. Biol. Chem. 280, 33076-33082.
    • (2005) J. Biol. Chem , vol.280 , pp. 33076-33082
    • Byfield, M.P.1    Murray, J.T.2    Backer, J.M.3
  • 28
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. 7
    • Petiot, A., Ogier-Denis, E., Blommaart, E. F., Meijer, A. J., and Codogno, P. (2000) Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. 7. Biol. Chem. 275, 992-998.
    • (2000) Biol. Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 29
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3kinase/protein kinase B pathway
    • Arico, S., Petiot, A., Bauvy, C., et al. (2001) The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3kinase/protein kinase B pathway. J. Biol. Chem. 276, 35243-35246.
    • (2001) J. Biol. Chem , vol.276 , pp. 35243-35246
    • Arico, S.1    Petiot, A.2    Bauvy, C.3
  • 30
    • 0005677775 scopus 로고
    • 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen, P. O. and Gordon, P. B. (1982) 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc. Natl. Acad. Sci. USA 79, 1889-1892.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 31
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • Liang, X. H., Jackson, S., Seaman, M., et al. (1999) Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 402, 672-676.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3
  • 32
    • 0035032723 scopus 로고    scopus 로고
    • Beclinphosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara, A., Kabeya, Y., Ohsumi, Y., and Yoshimori, T. (2001) Beclinphosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2, 330-335.
    • (2001) EMBO Rep , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 33
    • 39049194057 scopus 로고    scopus 로고
    • The Evolutionarily Conserved Domain of Beclin 1 is Required for Vps34 Binding, Autophagy and Tumor Suppressor Function
    • Furuya, N., Yu, J., Byfield, M., Pattingre, S., and Levine, B. (2005) The Evolutionarily Conserved Domain of Beclin 1 is Required for Vps34 Binding, Autophagy and Tumor Suppressor Function. Autophagy 1, 46-52.
    • (2005) Autophagy , vol.1 , pp. 46-52
    • Furuya, N.1    Yu, J.2    Byfield, M.3    Pattingre, S.4    Levine, B.5
  • 34
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre, S., Tassa, A., Qu, X., et al. (2005) Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 122, 927-939.
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3
  • 35
    • 0347986620 scopus 로고    scopus 로고
    • Class III phosphoinositide 3-kinase-Beclinl complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes
    • Tassa, A., Roux, M. P., Attaix, D., and Bechet, D. M. (2003) Class III phosphoinositide 3-kinase-Beclinl complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes. Biochem. J. 376, 577-586.
    • (2003) Biochem. J , vol.376 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 36
    • 0034703021 scopus 로고    scopus 로고
    • Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin- independent signaling pathway
    • Mordier, S., Deval, C., Bechet, D., Tassa, A., and Ferrara, M. (2000) Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin- independent signaling pathway. J. Biol. Chem. 275, 29900-29906.
    • (2000) J. Biol. Chem , vol.275 , pp. 29900-29906
    • Mordier, S.1    Deval, C.2    Bechet, D.3    Tassa, A.4    Ferrara, M.5
  • 37
    • 1542289063 scopus 로고    scopus 로고
    • Amino acids and insulin control autophagic proteolysis through different signaling pathways in relation to mTOR in isolated rat hepatocytes
    • Kanazawa, T., Taneike, I., Akaishi, R., et al. (2004) Amino acids and insulin control autophagic proteolysis through different signaling pathways in relation to mTOR in isolated rat hepatocytes. J. Biol. Chem. 279, 8452-8459.
    • (2004) J. Biol. Chem , vol.279 , pp. 8452-8459
    • Kanazawa, T.1    Taneike, I.2    Akaishi, R.3
  • 39
    • 10044219517 scopus 로고    scopus 로고
    • Amino acids and leucine allow insulin activation of the PKB/mTOR pathway in normal adipocytes treated with wortmannin and in adipocytes from db/db mice
    • Hinault, C., Mothe-Satney, I., Gautier, N., Lawrence, J. C., Jr., and van Obberghen, E. (2004) Amino acids and leucine allow insulin activation of the PKB/mTOR pathway in normal adipocytes treated with wortmannin and in adipocytes from db/db mice. FASEB J. 18, 1894-1896.
    • (2004) FASEB J , vol.18 , pp. 1894-1896
    • Hinault, C.1    Mothe-Satney, I.2    Gautier, N.3    Lawrence Jr., J.C.4    van Obberghen, E.5
  • 40
    • 14344254476 scopus 로고    scopus 로고
    • Inhibition of wortmannin activities by amino compounds
    • Isosaki M. (2004) Inhibition of wortmannin activities by amino compounds. Biochem. Biophys. Res. Commun. 324, 1406-1412.
    • (2004) Biochem. Biophys. Res. Commun , vol.324 , pp. 1406-1412
    • Isosaki, M.1
  • 41
    • 0034683568 scopus 로고    scopus 로고
    • Tor-mediated induction of autophagy via an Apg1 protein kinase complex
    • Kamada, Y., Funakoshi, T., Shintani, T., Nagano, K., Ohsumi, M., and Ohsumi, Y. (2000) Tor-mediated induction of autophagy via an Apg1 protein kinase complex. J. Cell Biol. 150, 1507-1513.
    • (2000) J. Cell Biol , vol.150 , pp. 1507-1513
    • Kamada, Y.1    Funakoshi, T.2    Shintani, T.3    Nagano, K.4    Ohsumi, M.5    Ohsumi, Y.6
  • 42
    • 18244394277 scopus 로고    scopus 로고
    • Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy
    • Kabeya, Y., Kamada, Y., Baba, M., Takikawa, H., Sasaki, M., and Ohsumi, Y. (2005) Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy. Mol. Biol. Cell 16, 2544-2553.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2544-2553
    • Kabeya, Y.1    Kamada, Y.2    Baba, M.3    Takikawa, H.4    Sasaki, M.5    Ohsumi, Y.6
  • 44
    • 0347627140 scopus 로고    scopus 로고
    • Amino acid signalling and the integration of metabolism
    • Meijer, A. J. and Dubbelhuis, P. F. (2004) Amino acid signalling and the integration of metabolism. Biochem. Biophys. Res. Commun. 313, 397-403.
    • (2004) Biochem. Biophys. Res. Commun , vol.313 , pp. 397-403
    • Meijer, A.J.1    Dubbelhuis, P.F.2
  • 45
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
    • Kahn, B. B., Alquier, T., Carling, D., and Hardie, D. G. (2005) AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 1, 15-25.
    • (2005) Cell Metab , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 46
    • 3042818799 scopus 로고    scopus 로고
    • Regulation of the TSC pathway by LKB1 : Evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome
    • Corradetti, M. N., Inoki, K., Bardeesy, N., DePinho, R. A., and Guan, K. L. (2004) Regulation of the TSC pathway by LKB1 : evidence of a molecular link between tuberous sclerosis complex and Peutz-Jeghers syndrome. Genes Dev. 18, 1533-1538.
    • (2004) Genes Dev , vol.18 , pp. 1533-1538
    • Corradetti, M.N.1    Inoki, K.2    Bardeesy, N.3    DePinho, R.A.4    Guan, K.L.5
  • 47
    • 1942469564 scopus 로고    scopus 로고
    • Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status
    • Cheng, S. W., Fryer, L. G., Carling, D., and Shepherd, P. R. (2004) Thr2446 is a novel mammalian target of rapamycin (mTOR) phosphorylation site regulated by nutrient status. J. Biol. Chem. 279, 15719-15722.
    • (2004) J. Biol. Chem , vol.279 , pp. 15719-15722
    • Cheng, S.W.1    Fryer, L.G.2    Carling, D.3    Shepherd, P.R.4
  • 48
    • 0034898851 scopus 로고    scopus 로고
    • Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p
    • Wang, Z., Wilson, W. A., Fujino, M. A., and Roach, P. J. (2001) Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p. Mol. Cell Biol. 21, 5742-5752.
    • (2001) Mol. Cell Biol , vol.21 , pp. 5742-5752
    • Wang, Z.1    Wilson, W.A.2    Fujino, M.A.3    Roach, P.J.4
  • 49
    • 0032508564 scopus 로고    scopus 로고
    • Inhibition of hepatocytic autophagy by adenosine, aminoimidazole-4-carboxamide riboside, and N6-mercaptopurine riboside. Evidence for involvement of amp-activated protein kinase
    • Samari, H. R. and Seglen, P. O. (1998) Inhibition of hepatocytic autophagy by adenosine, aminoimidazole-4-carboxamide riboside, and N6-mercaptopurine riboside. Evidence for involvement of amp-activated protein kinase. J. Biol. Chem. 273, 23758-23763.
    • (1998) J. Biol. Chem , vol.273 , pp. 23758-23763
    • Samari, H.R.1    Seglen, P.O.2
  • 50
    • 27644575235 scopus 로고    scopus 로고
    • Macroautophagy versus mitochondrial autophagy: A question of fate?
    • Kundu M. and Thompson C. B. (2005) Macroautophagy versus mitochondrial autophagy: a question of fate? Cell Death. Differ. 12., 1484-1489.
    • (2005) Cell Death. Differ , vol.12 , pp. 1484-1489
    • Kundu, M.1    Thompson, C.B.2
  • 51
    • 33644606491 scopus 로고    scopus 로고
    • Tracker dyes to probe mitochondrial autophagy (mitophagy) in rat hepatocytes
    • Rodriguez-Enriquez S., Kim I., Currin R. T., and Lemasters J. J. (2006) Tracker dyes to probe mitochondrial autophagy (mitophagy) in rat hepatocytes. Autophagy 2, 39-46.
    • (2006) Autophagy , vol.2 , pp. 39-46
    • Rodriguez-Enriquez, S.1    Kim, I.2    Currin, R.T.3    Lemasters, J.J.4
  • 53
    • 20444363122 scopus 로고    scopus 로고
    • The coordinate regulation of the p53 and mTOR pathways in cells
    • Feng, Z., Zhang, H., Levine, A. J., and Jin, S. (2005) The coordinate regulation of the p53 and mTOR pathways in cells. Proc. Natl. Acad. Sci. USA 102, 8204-8209.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8204-8209
    • Feng, Z.1    Zhang, H.2    Levine, A.J.3    Jin, S.4
  • 54
    • 32044435126 scopus 로고    scopus 로고
    • Coordination and communication between the p53 and IGF-1-AKT-TOR signal transduction pathways
    • Levine, A. J., Feng, Z., Mak, T. W., You, H., and Jin, S. (2006) Coordination and communication between the p53 and IGF-1-AKT-TOR signal transduction pathways. Genes Dev. 20, 267-275.
    • (2006) Genes Dev , vol.20 , pp. 267-275
    • Levine, A.J.1    Feng, Z.2    Mak, T.W.3    You, H.4    Jin, S.5
  • 55
    • 33645531089 scopus 로고    scopus 로고
    • Elongation factor-2 kinase regulates autophagy in human glioblastoma cells
    • Wu, H., Yang, J. M., Jin, S., Zhang, H., and Hait, W. N. (2006) Elongation factor-2 kinase regulates autophagy in human glioblastoma cells. Cancer Res. 66, 3015-3023.
    • (2006) Cancer Res , vol.66 , pp. 3015-3023
    • Wu, H.1    Yang, J.M.2    Jin, S.3    Zhang, H.4    Hait, W.N.5
  • 56
    • 1642328617 scopus 로고    scopus 로고
    • Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398
    • Browne, G. J., Finn, S. G., and Proud, C. G. (2004) Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. J. Biol. Chem. 279, 12220-12231.
    • (2004) J. Biol. Chem , vol.279 , pp. 12220-12231
    • Browne, G.J.1    Finn, S.G.2    Proud, C.G.3
  • 57
    • 33845924783 scopus 로고    scopus 로고
    • AMP-activated protein kinase and the regulation of autophagic proteolysis
    • Meley, D., Bauvy, C., Houben-Weerts, J. H., et al. (2006) AMP-activated protein kinase and the regulation of autophagic proteolysis. J. Biol. Chem. 281, 34870-34879.
    • (2006) J. Biol. Chem , vol.281 , pp. 34870-34879
    • Meley, D.1    Bauvy, C.2    Houben-Weerts, J.H.3
  • 58
    • 0035578226 scopus 로고    scopus 로고
    • Exogenous amino acids regulate trophectoderm differentiation in the mouse blastocyst through an mTORdependent pathway
    • Martin, P. M. and Sutherland, A. E. (2001) Exogenous amino acids regulate trophectoderm differentiation in the mouse blastocyst through an mTORdependent pathway. Dev. Biol. 240, 182-193.
    • (2001) Dev. Biol , vol.240 , pp. 182-193
    • Martin, P.M.1    Sutherland, A.E.2
  • 59
    • 0037662713 scopus 로고    scopus 로고
    • Regulation of targets of mTOR (mammalian target of rapamycin) signalling by intracellular amino acid availability
    • Beugnet, A., Tee, A. R., Taylor, P. M., and Proud, C. G. (2003) Regulation of targets of mTOR (mammalian target of rapamycin) signalling by intracellular amino acid availability. Biochem. J. 372, 555-566.
    • (2003) Biochem. J , vol.372 , pp. 555-566
    • Beugnet, A.1    Tee, A.R.2    Taylor, P.M.3    Proud, C.G.4
  • 60
    • 0034073638 scopus 로고    scopus 로고
    • Lynch, C. J., Fox, H. L., Vary, T. C., Jefferson, L. S., and Kimbal,l S. R. (2000) Regulation of amino acid-sensitive TOR signaling by leucine analogues in adipocytes. J. Cell Biochem. 77, 234-251.
    • Lynch, C. J., Fox, H. L., Vary, T. C., Jefferson, L. S., and Kimbal,l S. R. (2000) Regulation of amino acid-sensitive TOR signaling by leucine analogues in adipocytes. J. Cell Biochem. 77, 234-251.
  • 61
    • 0032971333 scopus 로고    scopus 로고
    • Structural requirement of leucine for activation of p70 S6 kinase
    • Shigemitsu, K., Tsujishita, Y., Miyaké, H., et al. (1999) Structural requirement of leucine for activation of p70 S6 kinase. FEBS Lett. 447, 303-306.
    • (1999) FEBS Lett , vol.447 , pp. 303-306
    • Shigemitsu, K.1    Tsujishita, Y.2    Miyaké, H.3
  • 62
    • 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
    • Smith, E. M., Finn, S. G., Tee, A. R., Browne, G. J., and Proud, C. G. (2005) 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. 280, 18717-18727.
    • (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
  • 63
    • 32244435285 scopus 로고    scopus 로고
    • Regulation of the small GTPase Rheb by amino acids
    • Roccio, M., Bos, J. L., and Zwartkruis, F. J. (2006) Regulation of the small GTPase Rheb by amino acids. Oncogene 25, 657-664.
    • (2006) Oncogene , vol.25 , pp. 657-664
    • Roccio, M.1    Bos, J.L.2    Zwartkruis, F.J.3
  • 64
    • 33644886769 scopus 로고    scopus 로고
    • Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation
    • Tzatsos, A. and Kandror, K. V. (2006) Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation. Mol. Cell Biol. 26, 63-76.
    • (2006) Mol. Cell Biol , vol.26 , pp. 63-76
    • Tzatsos, A.1    Kandror, K.V.2
  • 65
    • 21244456553 scopus 로고    scopus 로고
    • Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency
    • Long, X., Ortiz-Vega, S., Lin, Y., and Avruch, J. (2005) Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency. J. Biol. Chem. 280, 23433-23436.
    • (2005) J. Biol. Chem , vol.280 , pp. 23433-23436
    • Long, X.1    Ortiz-Vega, S.2    Lin, Y.3    Avruch, J.4
  • 66
    • 0141615891 scopus 로고    scopus 로고
    • Potential role of leucine metabolism in the leucine-signaling pathway involving mTOR
    • Lynch, C. J., Halle, B., Fujii, H., et al. (2003) Potential role of leucine metabolism in the leucine-signaling pathway involving mTOR. Am. J. Physiol. Endocrinol. Metab. 285, E854-E863.
    • (2003) Am. J. Physiol. Endocrinol. Metab , vol.285
    • Lynch, C.J.1    Halle, B.2    Fujii, H.3
  • 67
    • 0035145602 scopus 로고    scopus 로고
    • Metabolie regulation by leucine of translation initiation through the mTORsignaling pathway by pancreatic beta-cells
    • Xu, G., Kwon, G., Cruz, W. S., Marshall, C. A., and McDaniel, M. L. (2001) Metabolie regulation by leucine of translation initiation through the mTORsignaling pathway by pancreatic beta-cells. Diabetes 50, 353-360.
    • (2001) Diabetes , vol.50 , pp. 353-360
    • Xu, G.1    Kwon, G.2    Cruz, W.S.3    Marshall, C.A.4    McDaniel, M.L.5
  • 68
    • 0014421614 scopus 로고
    • Adenine nucleotide translocation of mitochondria. 1. Specificity and control
    • Pfaff, E. and Klingenberg, M. (1968) Adenine nucleotide translocation of mitochondria. 1. Specificity and control. Eur. J. Biochem. 6, 66-79.
    • (1968) Eur. J. Biochem , vol.6 , pp. 66-79
    • Pfaff, E.1    Klingenberg, M.2
  • 69
    • 0037012552 scopus 로고    scopus 로고
    • How does the mitochondrial ADP/ATP carrier distinguish transportable ATP and ADP from untransportable AMP and GTP?Dynamic modeling of the recognition/translocation process in the major substrate binding region
    • Goto, S., Chuman, H., Majima, E., and Terada, H. (2002) How does the mitochondrial ADP/ATP carrier distinguish transportable ATP and ADP from untransportable AMP and GTP?Dynamic modeling of the recognition/translocation process in the major substrate binding region. Biochim. Biophys. Acta 1589, 203-218.
    • (2002) Biochim. Biophys. Acta , vol.1589 , pp. 203-218
    • Goto, S.1    Chuman, H.2    Majima, E.3    Terada, H.4
  • 70
    • 0033403353 scopus 로고    scopus 로고
    • A novel human nucleoside diphosphate (NDP) kinase, Nm23-H6, localizes in mitochondria and affects cytokinesis
    • Tsuiki, H., Nitta, M., Furuya, A., et al. (1999) A novel human nucleoside diphosphate (NDP) kinase, Nm23-H6, localizes in mitochondria and affects cytokinesis. J. Cell Biochem. 76, 254-269.
    • (1999) J. Cell Biochem , vol.76 , pp. 254-269
    • Tsuiki, H.1    Nitta, M.2    Furuya, A.3
  • 71
    • 30344465756 scopus 로고    scopus 로고
    • Functional coupling between nucleoside diphosphate kinase of the outer mitochondrial compartment and oxidative phosphorylation
    • Lipskaya, T. Y. and Voinova, V. V. (2005) Functional coupling between nucleoside diphosphate kinase of the outer mitochondrial compartment and oxidative phosphorylation. Biochemistry (Mose.) 70, 1354-1362.
    • (2005) Biochemistry (Mose.) , vol.70 , pp. 1354-1362
    • Lipskaya, T.Y.1    Voinova, V.V.2
  • 72
    • 0025191311 scopus 로고    scopus 로고
    • Board, M., Humm, S., and Newsholme, E. A. (1990) Maximum activities of key enzymes of glycolysis, glutaminolysis, pentose phosphatepathway and tricarboxylic acid cycle in normal, neoplastic and suppressed cells. Biochem. J. 265, 503-509.
    • Board, M., Humm, S., and Newsholme, E. A. (1990) Maximum activities of key enzymes of glycolysis, glutaminolysis, pentose phosphatepathway and tricarboxylic acid cycle in normal, neoplastic and suppressed cells. Biochem. J. 265, 503-509.
  • 73
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval, R., Shvets, E., Fass, E., et al. (2007) Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 26, 1749-1760.
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3
  • 74
    • 33750071414 scopus 로고    scopus 로고
    • NF-{Kappa}B activation represses tumor necrosis factor-{alpha}-induced autophagy
    • Djavaheri-Mergny, M., Amelotti, M., Mathieu, J., et al. (2006) NF-{Kappa}B activation represses tumor necrosis factor-{alpha}-induced autophagy. J. Biol. Chem. 281, 30373-30382.
    • (2006) J. Biol. Chem , vol.281 , pp. 30373-30382
    • Djavaheri-Mergny, M.1    Amelotti, M.2    Mathieu, J.3
  • 75
    • 0031791670 scopus 로고    scopus 로고
    • Intracellular diadenosine polyphosphates: A novel second messenger in stimulus-secretion coupling
    • Martin, F., Pintor, J., Rovira, J. M., Ripoll, C., Miras-Portugal, M. T., and Soria, B. (1998) Intracellular diadenosine polyphosphates: a novel second messenger in stimulus-secretion coupling. FASEB J. 12, 1499-1506.
    • (1998) FASEB J , vol.12 , pp. 1499-1506
    • Martin, F.1    Pintor, J.2    Rovira, J.M.3    Ripoll, C.4    Miras-Portugal, M.T.5    Soria, B.6
  • 76
    • 0037007014 scopus 로고    scopus 로고
    • FKBP12-rapamycinassociated protein associates with mitochondria and senses osmotic stress via mitochondrial dysfunction
    • Desai, B. N., Myers, B. R., and Schreiber, S. L. (2002) FKBP12-rapamycinassociated protein associates with mitochondria and senses osmotic stress via mitochondrial dysfunction. Proc. Natl. Acad. Sci. USA 99, 4319-4324.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4319-4324
    • Desai, B.N.1    Myers, B.R.2    Schreiber, S.L.3
  • 77
    • 33748752151 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity
    • Schieke, S. M., Phillips, D., McCoy ,J. P., Jr., et al. (2006) The mammalian target of rapamycin (mTOR) pathway regulates mitochondrial oxygen consumption and oxidative capacity. J. Biol. Chem. 281, 27643-27652.
    • (2006) J. Biol. Chem , vol.281 , pp. 27643-27652
    • Schieke, S.M.1    Phillips, D.2    McCoy Jr., J.P.3
  • 78
    • 0027979626 scopus 로고
    • Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues
    • Weekes, J., Hawley, S. A., Cortón, J., Shugar, D., and Hardie, D. G. (1994) Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues. Eur. J. Biochem. 219, 751-757.
    • (1994) Eur. J. Biochem , vol.219 , pp. 751-757
    • Weekes, J.1    Hawley, S.A.2    Cortón, J.3    Shugar, D.4    Hardie, D.G.5
  • 79
    • 0033635215 scopus 로고    scopus 로고
    • Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain
    • Dong, J., Qiu, H., Garcia-Barrio, M., Anderson, J., and Hinnebusch, A. G. (2000) Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Mol. Cell 6, 269-279.
    • (2000) Mol. Cell , vol.6 , pp. 269-279
    • Dong, J.1    Qiu, H.2    Garcia-Barrio, M.3    Anderson, J.4    Hinnebusch, A.G.5
  • 80
    • 0034973590 scopus 로고    scopus 로고
    • Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast
    • Natarajan, K., Meyer, M. R., Jackson, B. M., et al. (2001) Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast. Mol. Cell Biol. 21, 4347-4368.
    • (2001) Mol. Cell Biol , vol.21 , pp. 4347-4368
    • Natarajan, K.1    Meyer, M.R.2    Jackson, B.M.3
  • 81
    • 0037382865 scopus 로고    scopus 로고
    • Translations control by TOR and TAP42 through dephosphorylation of eIF2alpha kinase GCN2
    • Cherkasova, V. A. and Hinnebusch, A. G. (2003) Translations control by TOR and TAP42 through dephosphorylation of eIF2alpha kinase GCN2. Genes Dev. 17, 859-872.
    • (2003) Genes Dev , vol.17 , pp. 859-872
    • Cherkasova, V.A.1    Hinnebusch, A.G.2
  • 82
    • 0037039442 scopus 로고    scopus 로고
    • Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway
    • Talloczy, Z., Jiang, W., Virgin, H. W., et al. (2002) Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway. Proc. Natl. Acad. Sci. USA 99, 190-195.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 190-195
    • Talloczy, Z.1    Jiang, W.2    Virgin, H.W.3
  • 83
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • Fang, Y., Vilella-Bach, M., Bachmann, R., Flanigan, A., and Chen, J. (2001) Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 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
  • 84
    • 33645241260 scopus 로고    scopus 로고
    • The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle
    • Hornberger, T. A., Chu, W. K., Mak, Y. W., Hsiung, J. W., Huang, S. A., and Chien, S. (2006) The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle. Proc. Natl. Acad. Sci USA 103, 4741-4746.
    • (2006) Proc. Natl. Acad. Sci USA , vol.103 , pp. 4741-4746
    • Hornberger, T.A.1    Chu, W.K.2    Mak, Y.W.3    Hsiung, J.W.4    Huang, S.A.5    Chien, S.6
  • 85
    • 4544220704 scopus 로고    scopus 로고
    • Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
    • Um, S. H., Frigerio, F., Watanabe, M., et al. (2004) Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity. Nature 431, 200-205.
    • (2004) Nature , vol.431 , pp. 200-205
    • Um, S.H.1    Frigerio, F.2    Watanabe, M.3
  • 86
    • 14244256097 scopus 로고    scopus 로고
    • Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: Possible involvement in obesity-linked insulin resistance
    • Khamzina, L., Veilleux, A., Bergeron, S., and Marette, A. (2005) Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance. Endocrinology 146, 1473-1481.
    • (2005) Endocrinology , vol.146 , pp. 1473-1481
    • Khamzina, L.1    Veilleux, A.2    Bergeron, S.3    Marette, A.4
  • 87
    • 33744505375 scopus 로고    scopus 로고
    • Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1
    • Um, S. H., D'Alessio, D., and Thomas, G. (2006) Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1. Cell Metab 3, 393-402.
    • (2006) Cell Metab , vol.3 , pp. 393-402
    • Um, S.H.1    D'Alessio, D.2    Thomas, G.3
  • 88
    • 6344226632 scopus 로고    scopus 로고
    • Amino acid metabolism in the Zucker diabetic fatty rat: Effects of insulin resistance and of type 2 diabetes
    • Wijekoon, E. P., Skinner, C., Brosnan, M. E., and Brosnan, J. T. (2004) Amino acid metabolism in the Zucker diabetic fatty rat: effects of insulin resistance and of type 2 diabetes. Can. J. Physiol Pharmacol. 82, 506-514.
    • (2004) Can. J. Physiol Pharmacol , vol.82 , pp. 506-514
    • Wijekoon, E.P.1    Skinner, C.2    Brosnan, M.E.3    Brosnan, J.T.4
  • 89
    • 33747619854 scopus 로고    scopus 로고
    • Insulin resistance accelerates muscle protein degradation: Activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling
    • Wang, X., Hu, Z., Hu, J., Du, J., and Mitch, W. E. (2006) Insulin resistance accelerates muscle protein degradation: activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling. Endocrinology 147, 4160-4168.
    • (2006) Endocrinology , vol.147 , pp. 4160-4168
    • Wang, X.1    Hu, Z.2    Hu, J.3    Du, J.4    Mitch, W.E.5
  • 91
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in the Drosophila fat body
    • Scott, R. C., Schuldiner, O., and Neufeld, T. P. (2004) Role and regulation of starvation-induced autophagy in the Drosophila fat body. Dev. Cell. 7, 167-178.
    • (2004) Dev. Cell , vol.7 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3
  • 92
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar, B., Vacher, C., Berger, Z., et al. (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat. Genet. 36, 585-595.
    • (2004) Nat. Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3
  • 93
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto, A., Cremona, M. L., and Rothman, J. E. (2006) Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J. Cell Biol. 172, 719-731.
    • (2006) J. Cell Biol , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 94
    • 4344595626 scopus 로고    scopus 로고
    • Regulation and role of autophagy in mammalian cells
    • Meijer, A. J. and Codogno, P. (2004) Regulation and role of autophagy in mammalian cells. Int. J. Biochem. Cell Biol. 36, 2445-2462.
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 2445-2462
    • Meijer, A.J.1    Codogno, P.2
  • 95
    • 2442485884 scopus 로고    scopus 로고
    • Ceramide-mediated macroautophagy involves inhibition of protein kinase B and up-regulation of beclin 1
    • Scarlatti, F., Bauvy, C., Ventruti, A., et al. (2004) Ceramide-mediated macroautophagy involves inhibition of protein kinase B and up-regulation of beclin 1. J. Biol. Chem. 279, 18384-18391.
    • (2004) J. Biol. Chem , vol.279 , pp. 18384-18391
    • Scarlatti, F.1    Bauvy, C.2    Ventruti, A.3
  • 96
    • 14644417747 scopus 로고    scopus 로고
    • Ceramide down-regulates System A amino acid transport and protein synthesis in rat skeletal muscle cells
    • Hyde, R., Hajduch, E., Powell, D. J., Taylor, P. M., and Hundal, H. S. (2005) Ceramide down-regulates System A amino acid transport and protein synthesis in rat skeletal muscle cells. FASEB J. 19, 461-463.
    • (2005) FASEB J , vol.19 , pp. 461-463
    • Hyde, R.1    Hajduch, E.2    Powell, D.J.3    Taylor, P.M.4    Hundal, H.S.5
  • 97
    • 0032588907 scopus 로고    scopus 로고
    • Involvement of p38MAPK in the regulation of proteolysis by liver cell hydration
    • Häussinger, D., Schliess, F., Dombrowski, F., and vom Dahl, S. (1999) Involvement of p38MAPK in the regulation of proteolysis by liver cell hydration. Gastroenterology 116, 921-935.
    • (1999) Gastroenterology , vol.116 , pp. 921-935
    • Häussinger, D.1    Schliess, F.2    Dombrowski, F.3    vom Dahl, S.4
  • 98
    • 0038711645 scopus 로고    scopus 로고
    • Involvement of integrins in osmosensing and signaling toward autophagic proteolysis in rat liver
    • vom Dahl, S., Schliess, F., Reissmann, R., et al. (2003) Involvement of integrins in osmosensing and signaling toward autophagic proteolysis in rat liver. J. Biol. Chem. 278, 27088-27095.
    • (2003) J. Biol. Chem , vol.278 , pp. 27088-27095
    • vom Dahl, S.1    Schliess, F.2    Reissmann, R.3
  • 99
    • 2442674271 scopus 로고    scopus 로고
    • Involvement of integrins and Src in insulin signaling toward autophagic proteolysis in rat liver
    • Schliess, F., Reissmann, R., Reinehr, R., vom Dahl, S., and Häussinger, D. (2004) Involvement of integrins and Src in insulin signaling toward autophagic proteolysis in rat liver. J. Biol. Chem. 279, 21294-21301.
    • (2004) J. Biol. Chem , vol.279 , pp. 21294-21301
    • Schliess, F.1    Reissmann, R.2    Reinehr, R.3    vom Dahl, S.4    Häussinger, D.5
  • 100
    • 33644670987 scopus 로고    scopus 로고
    • Insulin-stimulated glucose uptake does not require p38 mitogen-activated protein kinase in adipose tissue or skeletal muscle
    • Turban, S., Beardmore, V. A., Carr, J. M., et al. (2005) Insulin-stimulated glucose uptake does not require p38 mitogen-activated protein kinase in adipose tissue or skeletal muscle. Diabetes 54, 3161-3168.
    • (2005) Diabetes , vol.54 , pp. 3161-3168
    • Turban, S.1    Beardmore, V.A.2    Carr, J.M.3
  • 102
    • 0027163450 scopus 로고
    • Cell swelling and the sensitivity of autophagic proteolysis to inhibition by amino acids in isolated rat hepatocytes
    • Meijer, A. J., Gustafson, L. A., Luiken, J. J., et al. (1993) Cell swelling and the sensitivity of autophagic proteolysis to inhibition by amino acids in isolated rat hepatocytes. Eur. J. Biochem. 215, 449-454.
    • (1993) Eur. J. Biochem , vol.215 , pp. 449-454
    • Meijer, A.J.1    Gustafson, L.A.2    Luiken, J.J.3
  • 103
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: Their role in cell survival and cell death
    • Codogno, P. and Meijer, A. J. (2005) Autophagy and signaling: their role in cell survival and cell death. Cell Death. Differ. 12, 1509-1518.
    • (2005) Cell Death. Differ , vol.12 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 104
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine, B. and Klionsky, D. J. (2004) Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 6, 463-477.
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 105
    • 25444440875 scopus 로고    scopus 로고
    • The role of autophagy in cancer development and response to therapy
    • Kondo, Y., Kanzawa, T., Sawaya, R., and Kondo, S. (2005) The role of autophagy in cancer development and response to therapy. Nat. Rev. Cancer 5, 726-734.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 726-734
    • Kondo, Y.1    Kanzawa, T.2    Sawaya, R.3    Kondo, S.4
  • 106
    • 23644443068 scopus 로고    scopus 로고
    • The significance of autophagy in cancer
    • Ng, G. and Huang, J. (2005) The significance of autophagy in cancer. Mol. Carcinog. 43, 183-187.
    • (2005) Mol. Carcinog , vol.43 , pp. 183-187
    • Ng, G.1    Huang, J.2
  • 107
    • 33646271855 scopus 로고    scopus 로고
    • A matter of life or death (or both): Understanding autophagy in cancer
    • Hait, W. N., Jin, S., and Yang, J. M. (2006) A matter of life or death (or both): understanding autophagy in cancer. Clin. Cancer Res. 12, 1961-1965.
    • (2006) Clin. Cancer Res , vol.12 , pp. 1961-1965
    • Hait, W.N.1    Jin, S.2    Yang, J.M.3
  • 110
    • 0037470501 scopus 로고    scopus 로고
    • The endocrine regulation of aging by insulin-like signals
    • Tatar, M., Bartke, A., and Antebi, A. (2003) The endocrine regulation of aging by insulin-like signals. Science 299, 1346-1351.
    • (2003) Science , vol.299 , pp. 1346-1351
    • Tatar, M.1    Bartke, A.2    Antebi, A.3
  • 111
    • 14844293962 scopus 로고    scopus 로고
    • The role of insulin and IGF-1 signaling in longevity
    • Katie, M. and Kahn, C. R. (2005) The role of insulin and IGF-1 signaling in longevity. Cell Mol. Life Sci. 62, 320-343.
    • (2005) Cell Mol. Life Sci , vol.62 , pp. 320-343
    • Katie, M.1    Kahn, C.R.2
  • 112
    • 0042691506 scopus 로고    scopus 로고
    • Autophagy genes are essential for dauer development and life-span extension in C. elegans
    • Melendez, A., Talloczy, Z., Seaman, M., Eskelinen, E. L., Hall, D. H., and Levine, B. (2003) Autophagy genes are essential for dauer development and life-span extension in C. elegans. Science 301, 1387-1391.
    • (2003) Science , vol.301 , pp. 1387-1391
    • Melendez, A.1    Talloczy, Z.2    Seaman, M.3    Eskelinen, E.L.4    Hall, D.H.5    Levine, B.6
  • 113
    • 24944481544 scopus 로고    scopus 로고
    • Suppression of aging in mice by the hormone Klotho
    • Kurosu, H., Yamamoto, M., Clark, J. D., et al. (2005) Suppression of aging in mice by the hormone Klotho. Science 309, 1829-1833.
    • (2005) Science , vol.309 , pp. 1829-1833
    • Kurosu, H.1    Yamamoto, M.2    Clark, J.D.3
  • 114
    • 33748316536 scopus 로고    scopus 로고
    • SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells
    • Haigis, M. C., Mostoslavsky, R., Haigis, K. M., et al. (2006) SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126, 941-954.
    • (2006) Cell , vol.126 , pp. 941-954
    • Haigis, M.C.1    Mostoslavsky, R.2    Haigis, K.M.3
  • 115
    • 12344305124 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and type 2 diabetes
    • Lowell, B. B. and Shulman, G. I. (2005) Mitochondrial dysfunction and type 2 diabetes. Science 307, 384-387.
    • (2005) Science , vol.307 , pp. 384-387
    • Lowell, B.B.1    Shulman, G.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.