메뉴 건너뛰기




Volumn 6, Issue 6, 2005, Pages 439-448

Autophagy in metazoans: Cell survival in the land of plenty

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR; PROTEIN KINASE B; TARGET OF RAPAMYCIN KINASE;

EID: 20344406240     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1660     Document Type: Review
Times cited : (681)

References (108)
  • 1
    • 0141920730 scopus 로고    scopus 로고
    • Rab7 prevents growth factor-independent survival by inhibiting cell-autonomous nutrient transporter expression
    • Edinger, A. L., Cinalli, R. M. & Thompson, C. B. Rab7 prevents growth factor-independent survival by inhibiting cell-autonomous nutrient transporter expression. Dev. Cell 5, 571-582 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 571-582
    • Edinger, A.L.1    Cinalli, R.M.2    Thompson, C.B.3
  • 2
    • 0032497842 scopus 로고    scopus 로고
    • The role of PI3-kinase in insulin action
    • Alessi, D. R. & Downes, C. P. The role of PI3-kinase in insulin action. Biochim. Biophys. Acta 1436, 151-164 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 151-164
    • Alessi, D.R.1    Downes, C.P.2
  • 3
    • 4544331713 scopus 로고    scopus 로고
    • Activation of PI3K is indispensable for interleukin 7-mediated viability, proliferation, glucose use and growth of T cell acute lymphoblastic leukemia cells
    • Barata, J. T. et al. Activation of PI3K is indispensable for interleukin 7-mediated viability, proliferation, glucose use and growth of T cell acute lymphoblastic leukemia cells. J. Exp. Med. 200, 659-669 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 659-669
    • Barata, J.T.1
  • 4
    • 2142752480 scopus 로고    scopus 로고
    • Cellular autophagy: Surrender, avoidance and subversion by microorganisms
    • Kirkegaard, K., Taylor, M. P. & Jackson, W. T. Cellular autophagy: surrender, avoidance and subversion by microorganisms. Nature Rev. Microbiol. 2, 301-314 (2004).
    • (2004) Nature Rev. Microbiol. , vol.2 , pp. 301-314
    • Kirkegaard, K.1    Taylor, M.P.2    Jackson, W.T.3
  • 5
    • 4344595626 scopus 로고    scopus 로고
    • Regulation and role of autophagy in mammalian cells
    • Meijer, A. J. & Codogno, P. Regulation and role of autophagy in mammalian cells. Int. J. Biochem. Cell Biol. 36, 2445-2462 (2004).
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2445-2462
    • Meijer, A.J.1    Codogno, P.2
  • 6
    • 0347626252 scopus 로고    scopus 로고
    • Autophagy: A regulated bulk degradation process inside cells
    • Yoshimori, T. Autophagy: a regulated bulk degradation process inside cells. Biochem. Biophys. Res. Commun. 313, 453-458 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 453-458
    • Yoshimori, T.1
  • 7
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine, B. & Klionsky, D. J. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 6, 463-477 (2004).
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 8
    • 2442482810 scopus 로고    scopus 로고
    • Autophagy as a cell death and tumor suppressor mechanism
    • Gozuacik, D. & Kimchi, A. Autophagy as a cell death and tumor suppressor mechanism. Oncogene 23, 2891-2906 (2004).
    • (2004) Oncogene , vol.23 , pp. 2891-2906
    • Gozuacik, D.1    Kimchi, A.2
  • 9
    • 0037005133 scopus 로고    scopus 로고
    • Autophagy in yeast: A review of the molecular machinery
    • Huang, W. P. & Klionsky, D. J. Autophagy in yeast: a review of the molecular machinery. Cell Struct. Funct. 27, 409-420 (2002).
    • (2002) Cell Struct. Funct. , vol.27 , pp. 409-420
    • Huang, W.P.1    Klionsky, D.J.2
  • 10
    • 0036569331 scopus 로고    scopus 로고
    • Yeast autophagosomes: De novo formation of a membrane structure
    • Noda, T., Suzuki, K. & Ohsumi, Y. Yeast autophagosomes: de novo formation of a membrane structure. Trends Cell Biol. 12, 231-235 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 231-235
    • Noda, T.1    Suzuki, K.2    Ohsumi, Y.3
  • 11
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. Molecular dissection of autophagy: two ubiquitin-like systems. Nature Rev. Mol. Cell Biol. 2, 211-216 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 12
    • 0037004931 scopus 로고    scopus 로고
    • Diversity of signaling controls of macroautophagy in mammalian cells
    • Petiot, A. et al. Diversity of signaling controls of macroautophagy in mammalian cells. Cell Struct. Funct. 27, 431-441 (2002).
    • (2002) Cell Struct. Funct. , vol.27 , pp. 431-441
    • Petiot, A.1
  • 13
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada, M. & Ohsumi, Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333, 169-174 (1993). Shows the involvement of autophagy in maintaining survival of unicellular organisms during nutrient deprivation. Using a genetic screen to isolate yeast cells that are unable to form autophagic vacuoles, the authors identified the first set of autophagy genes, which provided the foundation for the discovery of homologues in higher eukaryotes.
    • (1993) FEBS Lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 14
    • 0037705403 scopus 로고    scopus 로고
    • Macroautophagy is required for multicellular development of the social amoeba Dictyostelium discoideum
    • Otto, G. P. et al. Macroautophagy is required for multicellular development of the social amoeba Dictyostelium discoideum. J. Biol. Chem. 278, 17636-17645 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 17636-17645
    • Otto, G.P.1
  • 15
    • 1842577042 scopus 로고    scopus 로고
    • Dictyostelium macroautophagy mutants vary in the severity of their developmental defects
    • Otto, G. P. et al. Dictyostelium macroautophagy mutants vary in the severity of their developmental defects. J. Biol. Chem. 279, 15621-15629 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 15621-15629
    • Otto, G.P.1
  • 16
    • 0023002623 scopus 로고
    • Biochemical changes during sucrose deprivation in higher plant cells
    • Journet, E. P., Bligny, R. & Douce, R. Biochemical changes during sucrose deprivation in higher plant cells. J. Biol. Chem. 261, 3193-3199 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 3193-3199
    • Journet, E.P.1    Bligny, R.2    Douce, R.3
  • 17
    • 0030003893 scopus 로고    scopus 로고
    • Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: Control by the supply of mitochondria with respiratory substrates
    • Aubert, S. et al. Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: control by the supply of mitochondria with respiratory substrates. J. Cell Biol. 133, 1251-1263 (1996). Work by the group in reference 16 showed that plants experience decreased glycolytic enzymatic activity, growth arrest and a decline in respiration during nutrient withdrawal. Reference 17 shows that autophagy is controlled by the levels of oxidizable substrates for the mitochondria and not by carbon sugar deprivation.
    • (1996) J. Cell Biol. , vol.133 , pp. 1251-1263
    • Aubert, S.1
  • 18
    • 0035983934 scopus 로고    scopus 로고
    • Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene
    • Hanaoka, H. et al. Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene. Plant Physiol. 129, 1181-1193 (2002).
    • (2002) Plant Physiol. , vol.129 , pp. 1181-1193
    • Hanaoka, H.1
  • 19
    • 14744268915 scopus 로고    scopus 로고
    • Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG 4s are essential for plant autophagy
    • Yoshimoto, K. et al. Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy. Plant Cell 16, 2967-2983 (2004).
    • (2004) Plant Cell , vol.16 , pp. 2967-2983
    • Yoshimoto, K.1
  • 20
    • 0037031843 scopus 로고    scopus 로고
    • The APG8/12-activating enzyme APG 7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana
    • Doelling, J. H., Walker, J. M., Friedman, E. M., Thompson, A. R. & Vierstra, R. D. The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana. J. Biol. Chem. 277, 33105-33114 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33105-33114
    • Doelling, J.H.1    Walker, J.M.2    Friedman, E.M.3    Thompson, A.R.4    Vierstra, R.D.5
  • 21
    • 0042691506 scopus 로고    scopus 로고
    • Autophagy genes are essential for dauer development and life-span extension in C. elegans
    • Melendez, A. et al. Autophagy genes are essential for dauer development and life-span extension in C. elegans. Science 301, 1387-1391 (2003).
    • (2003) Science , vol.301 , pp. 1387-1391
    • Melendez, A.1
  • 22
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in the Drosophila fat body
    • Scott, R. C., Schuldiner, O. & Neufeld, T. P. Role and regulation of starvation-induced autophagy in the Drosophila fat body. Dev. Cell 7, 167-178 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3
  • 23
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • Kuma, A. et al. The role of autophagy during the early neonatal starvation period. Nature 432, 963 (2004). Describes the first genetic demonstration for the in vivo requirement of autophagy in early neonatal mammal survival during nutrient starvation. Atg5-knockout neonatal mice have a severe reduction in the ability to survive up to the establishment of their ability to be nursed by their mothers. It follows from several observations (see references 24-27) that associated the degradation of glycogen in autophagosomes during early neonatal periods.
    • (2004) Nature , vol.432 , pp. 963
    • Kuma, A.1
  • 24
    • 0015251008 scopus 로고
    • Autophagic degradation of glycogen in skeletal muscles of the newborn rat
    • Schiaffino, S. & Hanzlikova, V. Autophagic degradation of glycogen in skeletal muscles of the newborn rat. J. Cell Biol. 52, 41-51 (1972).
    • (1972) J. Cell Biol. , vol.52 , pp. 41-51
    • Schiaffino, S.1    Hanzlikova, V.2
  • 25
    • 0019156179 scopus 로고
    • Random, presumably hydrolytic, and lysosomal glycogenolysis in the livers of rats treated with phlorizin and of newborn rats
    • Devos, P. & Hers, H. G. Random, presumably hydrolytic, and lysosomal glycogenolysis in the livers of rats treated with phlorizin and of newborn rats. Biochem. J. 192, 177-181 (1980).
    • (1980) Biochem. J. , vol.192 , pp. 177-181
    • Devos, P.1    Hers, H.G.2
  • 26
    • 0018854435 scopus 로고
    • Physicochemical and ultrastructural studies on glycogenosomes in newborn rat hepatocytes
    • Iwamasa, T., Tsuru, T., Hamada, T. & Takeuchi, T. Physicochemical and ultrastructural studies on glycogenosomes in newborn rat hepatocytes. Pathol. Res. Pract. 167, 363-373 (1980).
    • (1980) Pathol. Res. Pract. , vol.167 , pp. 363-373
    • Iwamasa, T.1    Tsuru, T.2    Hamada, T.3    Takeuchi, T.4
  • 27
    • 0345742550 scopus 로고    scopus 로고
    • An electron microscopic and biochemical study of the effects of glucagon on glycogen autophagy in the liver and heart of newborn rats
    • Kondomerkos, D. J., Kalamidas, S. A. & Kotoulas, O. B. An electron microscopic and biochemical study of the effects of glucagon on glycogen autophagy in the liver and heart of newborn rats. Microsc. Res. Tech. 63, 87-93 (2004).
    • (2004) Microsc. Res. Tech. , vol.63 , pp. 87-93
    • Kondomerkos, D.J.1    Kalamidas, S.A.2    Kotoulas, O.B.3
  • 28
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei, M. C. et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292, 727-730 (2001).
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1
  • 29
    • 2642536197 scopus 로고    scopus 로고
    • Alkylating DNA damage stimulates a regulated form of necrotic cell death
    • Zong, W. X. et al. Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes Dev. 18, 1272-1282 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 1272-1282
    • Zong, W.X.1
  • 30
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl- 2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong, W. X. et al. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15, 1481-1486 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 1481-1486
    • Zong, W.X.1
  • 31
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and survival in the absence of apoptosis
    • Lum, J. J. et al. Growth factor regulation of autophagy and survival in the absence of apoptosis. Cell 120, 237-248 (2005).
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.J.1
  • 32
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are invoked in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot, A. et al. Distinct classes of phosphatidylinositol 3′-kinases are invoked in signaling pathways that control macroautophagy in HT-29 cells. J. Biol. Chem. 275, 992-998 (2000). Shows that class-I and class-III PI3K cascades have distinct effects on autophagy. Autophagy can be blocked by class-I PI3K inhibitors, which allows new insight into the signal transduction cascades of how autophagy is regulated.
    • (2000) J. Biol. Chem. , vol.275 , pp. 992-998
    • Petiot, A.1
  • 33
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara, A. et al. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2, 330-335 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 330-335
    • Kihara, A.1
  • 34
    • 0021382386 scopus 로고
    • Haemopoietic cell growth factor mediates cell survival via its action on glucose transport
    • Whetton, A. D., Bazill, G. W. & Dexter, T. M. Haemopoietic cell growth factor mediates cell survival via its action on glucose transport. EMBO J. 3, 409-413 (1984).
    • (1984) EMBO J. , vol.3 , pp. 409-413
    • Whetton, A.D.1    Bazill, G.W.2    Dexter, T.M.3
  • 35
    • 0034904776 scopus 로고    scopus 로고
    • Growth factors can influence cell growth and survival through effects on glucose metabolism
    • Vander Heiden, M. G. et al. Growth factors can influence cell growth and survival through effects on glucose metabolism. Mol. Cell. Biol. 21, 5899-5912 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5899-5912
    • Vander Heiden, M.G.1
  • 36
    • 0036320205 scopus 로고    scopus 로고
    • Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake
    • Edinger, A. L. & Thompson, C. B. Akt maintains cell size and survival by increasing mTOR-dependent nutrient uptake. Mol. Biol. Cell 13, 2276-2288 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2276-2288
    • Edinger, A.L.1    Thompson, C.B.2
  • 37
    • 0141891296 scopus 로고    scopus 로고
    • Interleukin-3-mediated cell survival signals include phosphatidylinositol 3-kinase-dependent translocation of the glucose transporter GLUT 1 to the cell surface
    • Bentley, J. et al. Interleukin-3-mediated cell survival signals include phosphatidylinositol 3-kinase-dependent translocation of the glucose transporter GLUT1 to the cell surface. J. Biol. Chem. 278, 39337-39348 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 39337-39348
    • Bentley, J.1
  • 38
    • 6344227760 scopus 로고    scopus 로고
    • Cytokine stimulation of aerobic glycolysis in hematopoietic cells exceeds proliferative demand
    • Bauer, D. E. et al. Cytokine stimulation of aerobic glycolysis in hematopoietic cells exceeds proliferative demand. FASEB J. 18, 1303-1305 (2004).
    • (2004) FASEB J. , vol.18 , pp. 1303-1305
    • Bauer, D.E.1
  • 39
    • 0027318432 scopus 로고
    • Fibroblast growth factor-dependent metabolism of hypoxanthine via the salvage pathway for purine synthesis in porcine aortic endothelial cells
    • Miral, S. et al. Fibroblast growth factor-dependent metabolism of hypoxanthine via the salvage pathway for purine synthesis in porcine aortic endothelial cells. Biochem. Pharmacol. 45, 1695-1701 (1993).
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 1695-1701
    • Miral, S.1
  • 40
    • 0023771514 scopus 로고
    • Evidence for early mitogenic stimulation of metabolic flux through phosphoribosyl pyrophosphate into nucleotides in Swiss 3T3 cells
    • Ishijima, S. et al. Evidence for early mitogenic stimulation of metabolic flux through phosphoribosyl pyrophosphate into nucleotides in Swiss 3T3 cells. J. Biochem. 104, 570-575 (1988).
    • (1988) J. Biochem. , vol.104 , pp. 570-575
    • Ishijima, S.1
  • 41
    • 0008817735 scopus 로고    scopus 로고
    • Differential expression and regulation of nucleoside transport systems in rat liver parenchymal and hepatoma cells
    • del Santo, B. et al. Differential expression and regulation of nucleoside transport systems in rat liver parenchymal and hepatoma cells. Hepatology 28, 1504-1511 (1998).
    • (1998) Hepatology , vol.28 , pp. 1504-1511
    • Del Santo, B.1
  • 42
    • 0020730259 scopus 로고
    • Mitogenic enhancement of purine base phosphoribosylation in Swiss mouse 3T3 cells
    • Becker, M. A., Dicker, P. & Rozengurt, E. Mitogenic enhancement of purine base phosphoribosylation in Swiss mouse 3T3 cells. Am. J. Physiol. 244, C288-C296 (1983).
    • (1983) Am. J. Physiol. , vol.244
    • Becker, M.A.1    Dicker, P.2    Rozengurt, E.3
  • 43
    • 0035853833 scopus 로고    scopus 로고
    • Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology
    • Plas, D. R. et al. Akt and Bcl-xL promote growth factor-independent survival through distinct effects on mitochondrial physiology. J. Biol. Chem. 276, 12041-12048 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 12041-12048
    • Plas, D.R.1
  • 44
    • 0141863388 scopus 로고    scopus 로고
    • Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival
    • Rathmell, J. C. et al. Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival. Mol. Cell. Biol. 23, 7315-7328 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7315-7328
    • Rathmell, J.C.1
  • 45
    • 2542561169 scopus 로고    scopus 로고
    • Akt stimulates aerobic glycolysis in cancer cells
    • Elstrom, R. L. et al. Akt stimulates aerobic glycolysis in cancer cells. Cancer Res. 64, 3892-3899 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 3892-3899
    • Elstrom, R.L.1
  • 46
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie, D. G., Carting, D. & Carlson, M. The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67, 821-855 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carting, D.2    Carlson, M.3
  • 47
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay, N. & Sonenberg, N. Upstream and downstream of mTOR. Genes Dev. 18, 1926-1945 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 48
    • 0030598885 scopus 로고    scopus 로고
    • A signaling pathway to translational control
    • Brown, E. J. & Schreiber, S. L. A signaling pathway to translational control. Cell 86, 517-520 (1996).
    • (1996) Cell , vol.86 , pp. 517-520
    • Brown, E.J.1    Schreiber, S.L.2
  • 51
    • 2342559981 scopus 로고    scopus 로고
    • The TOR pathway: A target for cancer therapy
    • Bjornsti, M. A. Houghton, P. J. The TOR pathway: a target for cancer therapy. Nature Rev. Cancer 4, 335-348 (2004).
    • (2004) Nature Rev. Cancer , vol.4 , pp. 335-348
    • Bjornsti, M.A.1    Houghton, P.J.2
  • 52
    • 2342545519 scopus 로고    scopus 로고
    • Target of rapamycin (TOR): An integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression
    • Fingar, D. C. & Blenis, J. Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression. Oncogene 23, 3151-3171 (2004).
    • (2004) Oncogene , vol.23 , pp. 3151-3171
    • Fingar, D.C.1    Blenis, J.2
  • 53
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee, A. R. et al. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr. Biol. 13, 1259-1268 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1259-1268
    • Tee, A.R.1
  • 54
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC 2 GAP activity and regulates mTOR signaling
    • Inoki, K. et al. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev. 17, 1829-1834 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1829-1834
    • Inoki, K.1
  • 55
    • 0035798097 scopus 로고    scopus 로고
    • Mammalian TOR: A homeostatic ATP sensor
    • Dennis, P. B. et al. Mammalian TOR: a homeostatic ATP sensor. Science 294, 1102-1105 (2001).
    • (2001) Science , vol.294 , pp. 1102-1105
    • Dennis, P.B.1
  • 56
    • 0036364274 scopus 로고    scopus 로고
    • Control of p70 ribosomal protein S6 kinase and acetyl-CoA carboxylase by AMP-activated protein kinase and protein phosphatases in isolated hepatocytes
    • Krause, U., Bertrand, L. & Hue, L. Control of p70 ribosomal protein S6 kinase and acetyl-CoA carboxylase by AMP-activated protein kinase and protein phosphatases in isolated hepatocytes, Eur. J. Biochem. 269, 3751-3759 (2002).
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3751-3759
    • Krause, U.1    Bertrand, L.2    Hue, L.3
  • 57
    • 0037134910 scopus 로고    scopus 로고
    • Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase
    • Dubbelhuis, P. F. & Meijer, A. J. Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase. FEBS Lett. 521, 39-42 (2002).
    • (2002) FEBS Lett. , vol.521 , pp. 39-42
    • Dubbelhuis, P.F.1    Meijer, A.J.2
  • 58
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster, D. R. et al. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J. Biol. Chem. 277, 23977-23980 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 23977-23980
    • Bolster, D.R.1
  • 59
    • 0037144405 scopus 로고    scopus 로고
    • Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes
    • Larsen, A. K. et al. Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes. J. Biol. Chem. 277, 34826-34835 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34826-34835
    • Larsen, A.K.1
  • 60
    • 0345167800 scopus 로고    scopus 로고
    • TSC 2 mediates cellular energy response to control cell growth and survival
    • Inoki, K., Zhu, T. & Guan, K. L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 115, 577-590 (2003).
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 61
    • 0036714127 scopus 로고    scopus 로고
    • Akt regulates growth by directly phosphorylating Tsc 2
    • Potter, C. J., Pedraza, L. G. & Xu, T. Akt regulates growth by directly phosphorylating Tsc2. Nature Cell Biol. 4, 658-665 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 658-665
    • Potter, C.J.1    Pedraza, L.G.2    Xu, T.3
  • 62
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S 6 is inhibitory for autophagy in isolated rat hepatocytes
    • Blommaart, E. F. et al. Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J. Biol. Chem. 270, 2320-2326 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2320-2326
    • Blommaart, E.F.1
  • 63
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • Noda, T. & Ohsumi, Y. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273, 3963-3966 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 64
    • 0034722378 scopus 로고    scopus 로고
    • Dissection of autophagosome biogenesis into distinct nucleation and expansion steps
    • Abeliovich, H. et al. Dissection of autophagosome biogenesis into distinct nucleation and expansion steps. J. Cell Biol. 151, 1025-1034 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 1025-1034
    • Abeliovich, H.1
  • 65
    • 0042322394 scopus 로고    scopus 로고
    • Autophagy in yeast: A TOR-mediated response to nutrient starvation
    • Kamada, Y., Sekito, T. & Ohsumi, Y. Autophagy in yeast: a TOR-mediated response to nutrient starvation. Curr. Top. Microbiol. Immunol. 279, 73-84 (2004).
    • (2004) Curr. Top. Microbiol. Immunol. , vol.279 , pp. 73-84
    • Kamada, Y.1    Sekito, T.2    Ohsumi, Y.3
  • 66
    • 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 Pho 85p
    • Wang, Z. 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).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5742-5752
    • Wang, Z.1
  • 67
    • 0041357164 scopus 로고    scopus 로고
    • BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
    • Danial, N. N. et al. BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424, 952-956 (2003).
    • (2003) Nature , vol.424 , pp. 952-956
    • Danial, N.N.1
  • 68
    • 0036310982 scopus 로고    scopus 로고
    • The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation
    • Peng, T., Golub, T. R. & Sabatini, D. M. The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation. Mol. Cell. Biol. 22, 5575-5584 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5575-5584
    • Peng, T.1    Golub, T.R.2    Sabatini, D.M.3
  • 69
    • 0035487007 scopus 로고    scopus 로고
    • The mitochondrial permeability transition initiates autophagy in rat hepatocytes
    • Elmore, S. P. et al. The mitochondrial permeability transition initiates autophagy in rat hepatocytes. FASEB J. 15, 2286-2287 (2001).
    • (2001) FASEB J. , vol.15 , pp. 2286-2287
    • Elmore, S.P.1
  • 70
    • 0348010284 scopus 로고    scopus 로고
    • Mechanisms of caspase-independent neuronal death: Energy depletion and free radical generation
    • Lang-Rollin, I. C. et al. Mechanisms of caspase-independent neuronal death: energy depletion and free radical generation. J. Neurosci. 23, 11015-11025 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 11015-11025
    • Lang-Rollin, I.C.1
  • 71
    • 0035814933 scopus 로고    scopus 로고
    • Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis
    • Xue, L., Fletcher, G. C. & Tolkovsky, A. M. Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis. Curr. Biol. 11, 361-365 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 361-365
    • Xue, L.1    Fletcher, G.C.2    Tolkovsky, A.M.3
  • 72
    • 0032504568 scopus 로고    scopus 로고
    • The mitochondrial permeability transition in cell death: A common mechanism in necrosis, apoptosis and autophagy
    • Lemasters, J. J. et al. The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochim. Biophys. Acta 1366, 177-196 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 177-196
    • Lemasters, J.J.1
  • 73
    • 4644273585 scopus 로고    scopus 로고
    • Uth 1p is involved in the autophagic degradation of mitochondria
    • Kissova, I. et al. Uth1p is involved in the autophagic degradation of mitochondria. J. Biol. Chem. 279, 39068-39074 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 39068-39074
    • Kissova, I.1
  • 74
    • 0043066614 scopus 로고    scopus 로고
    • Macropexophagy in Hansenula polymorpha: Facts and views
    • Kiel, J. A. et al. Macropexophagy in Hansenula polymorpha: facts and views. FEBS Lett. 549, 1-6 (2003).
    • (2003) FEBS Lett. , vol.549 , pp. 1-6
    • Kiel, J.A.1
  • 75
    • 0035977052 scopus 로고    scopus 로고
    • Peroxisome biogenesis and selective degradation converge at Pex 14p
    • Bellu, A. R. et al. Peroxisome biogenesis and selective degradation converge at Pex14p. J. Biol. Chem. 276, 44570-44574 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44570-44574
    • Bellu, A.R.1
  • 76
    • 2942518250 scopus 로고    scopus 로고
    • Lost in translation: Dysregulation of cap-dependent translation and cancer
    • Bjornsti, M. A. & Houghton, P. J. Lost in translation: dysregulation of cap-dependent translation and cancer. Cancer Cell 5, 519-523 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 519-523
    • Bjornsti, M.A.1    Houghton, P.J.2
  • 77
    • 0344063370 scopus 로고    scopus 로고
    • Will mTOR inhibitors make it as cancer drugs?
    • Sawyers, C. L. Will mTOR inhibitors make it as cancer drugs? Cancer Cell 4, 343-348 (2003).
    • (2003) Cancer Cell , vol.4 , pp. 343-348
    • Sawyers, C.L.1
  • 78
    • 9144240441 scopus 로고    scopus 로고
    • Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
    • Qu, X. et al. Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene. J. Clin. Invest. 112, 1809-1820 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 1809-1820
    • Qu, X.1
  • 79
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • Yue, Z. et al. Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc. Natl Acad. Sci. USA 100, 15077-15082 (2003). References 76 and 79 describe the first experimental evidence that genetic inactivation of beclin-1 resulted in a high frequency of tumour formation. These mice had both lower basal levels of autophagy and defective autophagic responses.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15077-15082
    • Yue, Z.1
  • 80
    • 0038743077 scopus 로고    scopus 로고
    • Induction of autophagic cell death in malignant glioma cells by arsenic trioxide
    • Kanzawa, T. et al. Induction of autophagic cell death in malignant glioma cells by arsenic trioxide. Cancer Res. 63, 2103-2108 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 2103-2108
    • Kanzawa, T.1
  • 81
    • 1842865745 scopus 로고    scopus 로고
    • Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells
    • Kanzawa, T. et al. Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells. Cell Death Differ. 11, 448-457 (2004).
    • (2004) Cell Death Differ. , vol.11 , pp. 448-457
    • Kanzawa, T.1
  • 82
    • 0035863399 scopus 로고    scopus 로고
    • A novel response of cancer cells to radiation involves autophagy and formation of acidic vesicles
    • Paglin, S. et al. A novel response of cancer cells to radiation involves autophagy and formation of acidic vesicles. Cancer Res. 61, 439-444 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 439-444
    • Paglin, S.1
  • 83
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death
    • Bursch, W. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ. 8, 569-581 (2001).
    • (2001) Cell Death Differ. , vol.8 , pp. 569-581
    • Bursch, W.1
  • 84
    • 2642553881 scopus 로고    scopus 로고
    • Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8
    • Yu, L. et al. Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science 304, 1500-1502 (2004). The authors describe how autophagic cell death is regulated by the caspase-8 pathway. Induction of autophagy by a general caspase inhibitor promotes autophagy and is prevented by knockdown of ATG7 and beclin-1.
    • (2004) Science , vol.304 , pp. 1500-1502
    • Yu, L.1
  • 85
    • 0038393057 scopus 로고    scopus 로고
    • The Drosophila homolog of Aut 1 is essential for autophagy and development
    • Juhasz, G. et al. The Drosophila homolog of Aut1 is essential for autophagy and development. FEBS Lett. 543, 154-158 (2003).
    • (2003) FEBS Lett. , vol.543 , pp. 154-158
    • Juhasz, G.1
  • 86
    • 0242499488 scopus 로고    scopus 로고
    • Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases
    • Zhu, J. H. et al. Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases. Brain Pathol. 13, 473-481 (2003).
    • (2003) Brain Pathol. , vol.13 , pp. 473-481
    • Zhu, J.H.1
  • 87
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis, L. et al. Expression of A53T mutant but not wild-type α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J. Neurosci. 21, 9549-9560 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 9549-9560
    • Stefanis, L.1
  • 88
    • 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. et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nature Genet. 36, 585-595 (2004).
    • (2004) Nature Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1
  • 89
    • 0348013126 scopus 로고    scopus 로고
    • Autophagy regulates the processing of amino terminal huntingtin fragments
    • Qin, Z. H. et al. Autophagy regulates the processing of amino terminal huntingtin fragments. Hum. Mol. Genet. 12, 3231-3244 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3231-3244
    • Qin, Z.H.1
  • 90
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade, P. et al. Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol. Histopathol. 12, 25-31 (1997).
    • (1997) Histol. Histopathol. , vol.12 , pp. 25-31
    • Anglade, P.1
  • 91
    • 0035364748 scopus 로고    scopus 로고
    • Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration
    • Petersen, A. et al. Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration. Hum. Mol. Genet. 10, 1243-1254 (2001).
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1243-1254
    • Petersen, A.1
  • 92
    • 0043173825 scopus 로고    scopus 로고
    • Dopamine induces autophagic cell death and α-synuclein increase in human neuroblastoma SH-SY 5Y cells
    • Gomez-Santos, C. et al. Dopamine induces autophagic cell death and α-synuclein increase in human neuroblastoma SH-SY5Y cells. J. Neurosci. Res. 73, 341-350 (2003).
    • (2003) J. Neurosci. Res. , vol.73 , pp. 341-350
    • Gomez-Santos, C.1
  • 93
    • 8344247016 scopus 로고    scopus 로고
    • Autophagy defends cells against invading group A Streptococcus
    • Nakagawa, I. et al. Autophagy defends cells against invading group A Streptococcus. Science 306, 1037-1040 (2004).
    • (2004) Science , vol.306 , pp. 1037-1040
    • Nakagawa, I.1
  • 94
    • 0037711625 scopus 로고    scopus 로고
    • Cytoplasmic bacteria can be targets for autophagy
    • Rich, K. A., Burkett, C. & Webster, P. Cytoplasmic bacteria can be targets for autophagy. Cell. Microbiol. 5, 455-468 (2003).
    • (2003) Cell. Microbiol. , vol.5 , pp. 455-468
    • Rich, K.A.1    Burkett, C.2    Webster, P.3
  • 95
    • 13244256806 scopus 로고    scopus 로고
    • Escape of intracellular shigella from autophagy
    • Ogawa, M. et al. Escape of intracellular shigella from autophagy. Science 307, 727-731 (2004).
    • (2004) Science , vol.307 , pp. 727-731
    • Ogawa, M.1
  • 96
    • 2542628931 scopus 로고    scopus 로고
    • Ras is involved in the negative control of autophagy through the class I PI3-kinase
    • Furuta, S. et al. Ras is involved in the negative control of autophagy through the class I PI3-kinase. Oncogene 23, 3898-3904 (2004).
    • (2004) Oncogene , vol.23 , pp. 3898-3904
    • Furuta, S.1
  • 97
    • 0042326145 scopus 로고    scopus 로고
    • c-myc induces autophagy in rat 3Y1 fibroblast cells
    • Tsuneoka, M. et al. c-myc induces autophagy in rat 3Y1 fibroblast cells. Cell Struct. Funct. 28, 195-204 (2003).
    • (2003) Cell Struct. Funct. , vol.28 , pp. 195-204
    • Tsuneoka, M.1
  • 98
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway
    • Arico, S. et al. The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway. J. Biol. Chem. 276, 35243-35246 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35243-35246
    • Arico, S.1
  • 99
    • 0035870257 scopus 로고    scopus 로고
    • Beclin 1 contains a leucine-rich nuclear export signal that is required for its autophagy and tumor suppressor function
    • Liang, X. H. et al. Beclin 1 contains a leucine-rich nuclear export signal that is required for its autophagy and tumor suppressor function. Cancer Res. 61, 3443-3449 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 3443-3449
    • Liang, X.H.1
  • 100
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber, S. L. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 251, 283-287 (1991).
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 101
    • 10344262564 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
    • Shimizu, S. et al. Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes. Nature Cell Biol. 6, 1221-1228 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 1221-1228
    • Shimizu, S.1
  • 102
    • 0029741890 scopus 로고    scopus 로고
    • Active cell death induced by the anti-estrogens tamoxifen and ICI 164 384 in human mammary carcinoma cells (MCF-7) in culture: The role of autophagy
    • Bursch, W. et al. Active cell death induced by the anti-estrogens tamoxifen and ICI 164 384 in human mammary carcinoma cells (MCF-7) in culture: the role of autophagy. Carcinogenesis 17, 1595-1607 (1996).
    • (1996) Carcinogenesis , vol.17 , pp. 1595-1607
    • Bursch, W.1
  • 103
    • 0037440032 scopus 로고    scopus 로고
    • Ceramide: Second messenger or modulator of membrane structure and dynamics?
    • van Blitterswijk, W. J. et al. Ceramide: second messenger or modulator of membrane structure and dynamics? Biochem. J. 369, 199-211 (2003).
    • (2003) Biochem. J. , vol.369 , pp. 199-211
    • Van Blitterswijk, W.J.1
  • 104
    • 6944241423 scopus 로고    scopus 로고
    • Sphingosine-dependent apoptosis: A unified concept based on multiple mechanisms operating in concert
    • Suzuki, E. et al. Sphingosine-dependent apoptosis: a unified concept based on multiple mechanisms operating in concert. Proc. Natl. Acad. Sci. USA 101, 14788-14793 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14788-14793
    • Suzuki, E.1
  • 105
    • 2442485884 scopus 로고    scopus 로고
    • Ceramide-mediated macroautophagy involves inhibition of protein kinase B and up-regulation of beclin 1
    • Scarlatti, F. et al. Ceramide-mediated macroautophagy involves inhibition of protein kinase B and up-regulation of beclin 1. J. Biol. Chem. 279, 18384-18391 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 18384-18391
    • Scarlatti, F.1
  • 106
    • 3042562282 scopus 로고    scopus 로고
    • Pivotal role of the cell death factor BNIP3 in ceramide-induced autophagic cell death in malignant glioma cells
    • Daido, S. et al. Pivotal role of the cell death factor BNIP3 in ceramide-induced autophagic cell death in malignant glioma cells. Cancer Res. 64, 4286-4293 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 4286-4293
    • Daido, S.1
  • 107
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima, N. et al. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol. Biol. Cell 15, 1101-1111 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1
  • 108
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya, Y. et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 19, 5720-5728 (2000). References 107 and 108 describe the mammalian homologue of ATGB, LC3, as a specific marker of autophagosome formation.
    • (2000) EMBO J. , vol.19 , pp. 5720-5728
    • Kabeya, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.