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Volumn 11, Issue 3, 2014, Pages 187-200

Liver autophagy: Much more than just taking out the trash

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; CHAPERONE; LIVER ENZYME; PARACETAMOL;

EID: 84895930872     PISSN: 17595045     EISSN: 17595053     Source Type: Journal    
DOI: 10.1038/nrgastro.2013.211     Document Type: Review
Times cited : (160)

References (165)
  • 1
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., Levine, B., Cuervo, A. M. & Klionsky, D. J. Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075 (2008).
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 2
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang, Z. & Klionsky, D. J. Mammalian autophagy: core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 22, 124-131 (2010).
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 3
    • 82755187338 scopus 로고
    • Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover, A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Biochim. Biophys. Acta 1824, 3-13 (2012).
    • (1824) Biochim. Biophys. Acta , pp. 3-13
    • Ciechanover, A.1
  • 5
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: Implications for metabolism
    • Mizushima, N. & Klionsky, D. J. Protein turnover via autophagy: implications for metabolism. Annu. Rev. Nutr. 27, 19-40 (2007).
    • (2007) Annu. Rev. Nutr. , vol.27 , pp. 19-40
    • Mizushima, N.1    Klionsky, D.J.2
  • 6
    • 79955631150 scopus 로고    scopus 로고
    • Autophagy in the cellular energetic balance
    • Singh, R. & Cuervo, A. M. Autophagy in the cellular energetic balance. Cell Metab. 13, 495-504 (2011).
    • (2011) Cell Metab. , vol.13 , pp. 495-504
    • Singh, R.1    Cuervo, A.M.2
  • 7
    • 0014148066 scopus 로고
    • Participation of lysosomes in cellular autophagy induced in rat liver by glucagon
    • Deter, R. L., Baudhuin, P. & De Duve, C. Participation of lysosomes in cellular autophagy induced in rat liver by glucagon. J. Cell Biol. 35, C11-C16 (1967).
    • (1967) J. Cell Biol. , vol.35
    • Deter, R.L.1    Baudhuin, P.2    De Duve, C.3
  • 8
    • 0017697151 scopus 로고
    • Induction of autophagy by amino-acid deprivation in perfused rat liver
    • Mortimore, G. E. & Schworer, C. M. Induction of autophagy by amino-acid deprivation in perfused rat liver. Nature 270, 174-176 (1977).
    • (1977) Nature , vol.270 , pp. 174-176
    • Mortimore, G.E.1    Schworer, C.M.2
  • 9
    • 0014939582 scopus 로고
    • Inhibition by insulin of valine turnover in liver
    • Mortimore, G. & Mondon, C. E. Inhibition by insulin of valine turnover in liver. J. Biol. Chem. 245, 2375-2383 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 2375-2383
    • Mortimore, G.1    Mondon, C.E.2
  • 10
    • 10744225487 scopus 로고    scopus 로고
    • A unified nomenclature for yeast autophagy-related genes
    • Klionsky, D. J. et al. A unified nomenclature for yeast autophagy-related genes. Dev. Cell 5, 539-545 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 539-545
    • Klionsky, D.J.1
  • 11
    • 0032545292 scopus 로고    scopus 로고
    • A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy
    • Mizushima, N., Sugita, H., Yoshimori, T. & Ohsumi, Y. A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy. J. Biol. Chem. 273, 33889-33892 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33889-33892
    • Mizushima, N.1    Sugita, H.2    Yoshimori, T.3    Ohsumi, Y.4
  • 13
    • 79952356168 scopus 로고    scopus 로고
    • Autophagy receptors in developmental clearance of mitochondria
    • Novak, I. & Dikic, I. Autophagy receptors in developmental clearance of mitochondria. Autophagy 7, 301-303 (2011).
    • (2011) Autophagy , vol.7 , pp. 301-303
    • Novak, I.1    Dikic, I.2
  • 15
    • 0032555641 scopus 로고    scopus 로고
    • Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes
    • Berg, T. O., Fengsrud, M., Stromhaug, P. E., Berg, T. & Seglen, P. O. Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes. J. Biol. Chem. 273, 21883-21892 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 21883-21892
    • Berg, T.O.1    Fengsrud, M.2    Stromhaug, P.E.3    Berg, T.4    Seglen, P.O.5
  • 16
    • 33947369047 scopus 로고    scopus 로고
    • Permeases recycle amino acids resulting from autophagy
    • Yang, Z. & Klionsky, D. J. Permeases recycle amino acids resulting from autophagy. Autophagy 3, 149-150 (2007).
    • (2007) Autophagy , vol.3 , pp. 149-150
    • Yang, Z.1    Klionsky, D.J.2
  • 17
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase
    • Zoncu, R. et al. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 334, 678-683 (2011).
    • (2011) Science , vol.334 , pp. 678-683
    • Zoncu, R.1
  • 18
    • 21044455137 scopus 로고    scopus 로고
    • Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice
    • Komatsu, M. et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169, 425-434 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 425-434
    • Komatsu, M.1
  • 19
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto, A., Cremona, M. & Rothman, J. Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J. Cell Biol. 172, 719-731 (2006).
    • (2006) J. Cell Biol. , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.2    Rothman, J.3
  • 20
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G., Marino, G. & Levine, B. Autophagy and the integrated stress response. Mol. Cell 40, 280-293 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 22
    • 0032482219 scopus 로고    scopus 로고
    • Peroxisome degradation by microautophagy in Pichia pastoris. Identification of specific steps and morphological intermediates
    • Sakai, Y., Koller, A., Rangell, L., Keller, G. & Subramani, S. Peroxisome degradation by microautophagy in Pichia pastoris. Identification of specific steps and morphological intermediates. J. Cell Biol. 141, 625-636 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 625-636
    • Sakai, Y.1    Koller, A.2    Rangell, L.3    Keller, G.4    Subramani, S.5
  • 23
    • 78651423598 scopus 로고    scopus 로고
    • Microautophagy of cytosolic proteins by late endosomes
    • Sahu, R. et al. Microautophagy of cytosolic proteins by late endosomes. Dev. Cell 20, 131-139 (2011).
    • (2011) Dev. Cell , vol.20 , pp. 131-139
    • Sahu, R.1
  • 24
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C. & Stenmark, H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452 (2009).
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 25
    • 35348869859 scopus 로고    scopus 로고
    • ESCRTs and Fab1 regulate distinct steps of autophagy
    • Rusten, T. E. et al. ESCRTs and Fab1 regulate distinct steps of autophagy. Curr. Biol. 17, 1817-1825 (2007).
    • (2007) Curr. Biol. , vol.17 , pp. 1817-1825
    • Rusten, T.E.1
  • 26
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice, J. F. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem. Sci. 15, 305-309 (1990).
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 27
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • Bandyopadhyay, U., Kaushik, S., Varticovski, L. & Cuervo, A. M. The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol. Cell. Biol. 28, 5747-5763 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 28
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A. M. & Dice, J. F. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273, 501-503 (1996).
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 29
    • 84869498101 scopus 로고    scopus 로고
    • Chaperones in autophagy
    • Kaushik, S. & Cuervo, A. M. Chaperones in autophagy. Pharmacol. Res. 66, 484-493 (2012).
    • (2012) Pharmacol. Res. , vol.66 , pp. 484-493
    • Kaushik, S.1    Cuervo, A.M.2
  • 30
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: A unique way to enter the lysosome world
    • Kaushik, S. & Cuervo, A. M. Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell. Biol. 22, 407-417 (2012).
    • (2012) Trends Cell. Biol. , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 31
    • 79954422997 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in protein quality control
    • Arias, E. & Cuervo, A. M. Chaperone-mediated autophagy in protein quality control. Curr. Opin. Cell Biol. 23, 184-189 (2011).
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 184-189
    • Arias, E.1    Cuervo, A.M.2
  • 32
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • Kiffin, R., Christian, C. J., Knecht, E. & Cuervo, A. M. Activation of chaperone-mediated autophagy during oxidative stress. Mol. Biol. Cell 15, 4829-4840 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.J.2    Knecht, E.3    Cuervo, A.M.4
  • 34
    • 34147168105 scopus 로고    scopus 로고
    • Distinct roles of autophagy in the heart during ischemia and reperfusion: Roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy
    • Matsui, Y. et al. Distinct roles of autophagy in the heart during ischemia and reperfusion: roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy. Circ. Res. 100, 914-922 (2007).
    • (2007) Circ. Res. , vol.100 , pp. 914-922
    • Matsui, Y.1
  • 35
    • 77953861522 scopus 로고    scopus 로고
    • Ammonia derived from glutaminolysis is a diffusible regulator of autophagy
    • Eng, C. H., Yu, K., Lucas, J., White, E. & Abraham, R. T. Ammonia derived from glutaminolysis is a diffusible regulator of autophagy. Sci. Signal. 3, ra31 (2010).
    • (2010) Sci. Signal. , vol.3
    • Eng, C.H.1    Yu, K.2    Lucas, J.3    White, E.4    Abraham, R.T.5
  • 36
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and cell survival in the absence of apoptosis
    • Lum, J. et al. Growth factor regulation of autophagy and cell survival in the absence of apoptosis. Cell 120, 237-248 (2005).
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.1
  • 37
    • 79959952405 scopus 로고    scopus 로고
    • Liver autophagy contributes to the maintenance of blood glucose and amino acid levels
    • Ezaki, J. et al. Liver autophagy contributes to the maintenance of blood glucose and amino acid levels. Autophagy 7, 727-736 (2011).
    • (2011) Autophagy , vol.7 , pp. 727-736
    • Ezaki, J.1
  • 38
    • 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, 1032-1036 (2004).
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1
  • 39
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo, A. M., Knecht, E., Terlecky, S. R. & Dice, J. F. Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am. J. Physiol. 269, C1200-C1208 (1995).
    • (1995) Am. J. Physiol. , vol.269
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 40
    • 84879121285 scopus 로고    scopus 로고
    • Chemical modulation of chaperone-mediated autophagy by retinoic acid derivatives
    • Anguiano, J. et al. Chemical modulation of chaperone-mediated autophagy by retinoic acid derivatives. Nat. Chem. Biol. 9, 374-382 (2013).
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 374-382
    • Anguiano, J.1
  • 41
    • 21844440290 scopus 로고    scopus 로고
    • Ketone bodies stimulate chaperone-mediated autophagy
    • Finn, P. F. & Dice, J. F. Ketone bodies stimulate chaperone-mediated autophagy. J. Biol. Chem. 280, 25864-25870 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 25864-25870
    • Finn, P.F.1    Dice, J.F.2
  • 42
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo, A. M. & Dice, J. F. Regulation of lamp2a levels in the lysosomal membrane. Traffic 1, 570-583 (2000).
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.M.1    Dice, J.F.2
  • 43
    • 65949095803 scopus 로고    scopus 로고
    • Autophagy regulates lipid metabolism
    • Singh, R. et al. Autophagy regulates lipid metabolism. Nature 458, 1131-1135 (2009).
    • (2009) Nature , vol.458 , pp. 1131-1135
    • Singh, R.1
  • 44
    • 78049467743 scopus 로고    scopus 로고
    • Autophagy reduces acute ethanol-induced hepatotoxicity and steatosis in mice
    • Ding, W. X. et al. Autophagy reduces acute ethanol-induced hepatotoxicity and steatosis in mice. Gastroenterology 139, 1740-1752 (2010).
    • (2010) Gastroenterology , vol.139 , pp. 1740-1752
    • Ding, W.X.1
  • 45
    • 80054788704 scopus 로고    scopus 로고
    • Differential roles of unsaturated and saturated fatty acids on autophagy and apoptosis in hepatocytes
    • Mei, S. et al. Differential roles of unsaturated and saturated fatty acids on autophagy and apoptosis in hepatocytes. J. Pharmacol. Exp. Ther. 339, 487-498 (2011).
    • (2011) J. Pharmacol. Exp. Ther. , vol.339 , pp. 487-498
    • Mei, S.1
  • 46
    • 84878533962 scopus 로고    scopus 로고
    • MXL-3 and HLH-30 transcriptionally link lipolysis and autophagy to nutrient availability
    • O'Rourke, E. J. & Ruvkun, G. MXL-3 and HLH-30 transcriptionally link lipolysis and autophagy to nutrient availability. Nat. Cell Biol. 15, 668-676 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 668-676
    • O'Rourke, E.J.1    Ruvkun, G.2
  • 47
    • 80053312481 scopus 로고    scopus 로고
    • Autophagy and lipid metabolism coordinately modulate life span in germline-less
    • Lapierre, L. R., Gelino, S., Melendez, A. & Hansen, M. Autophagy and lipid metabolism coordinately modulate life span in germline-less, C. elegans. Curr. Biol. 21, 1507-1514 (2011).
    • (2011) C. Elegans. Curr. Biol. , vol.21 , pp. 1507-1514
    • Lapierre, L.R.1    Gelino, S.2    Melendez, A.3    Hansen, M.4
  • 48
    • 84878606239 scopus 로고    scopus 로고
    • TFEB controls cellular lipid metabolism through a starvation-induced autoregulatory loop
    • Settembre, C. et al. TFEB controls cellular lipid metabolism through a starvation-induced autoregulatory loop. Nat. Cell Biol. 15, 647-658 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 647-658
    • Settembre, C.1
  • 49
    • 81355161371 scopus 로고    scopus 로고
    • A role for autophagy during hepatic stellate cell activation
    • Thoen, L. F. et al. A role for autophagy during hepatic stellate cell activation. J. Hepatol. 55, 1353-1360 (2011).
    • (2011) J. Hepatol. , vol.55 , pp. 1353-1360
    • Thoen, L.F.1
  • 50
    • 84859444880 scopus 로고    scopus 로고
    • Autophagy releases lipid that promotes fibrogenesis by activated hepatic stellate cells in mice and in human tissues
    • Hernandez-Gea, V. et al. Autophagy releases lipid that promotes fibrogenesis by activated hepatic stellate cells in mice and in human tissues. Gastroenterology 142, 938-946 (2012).
    • (2012) Gastroenterology , vol.142 , pp. 938-946
    • Hernandez-Gea, V.1
  • 52
    • 78049409236 scopus 로고    scopus 로고
    • Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism
    • Jiang, S. et al. Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism. J. Biol. Chem. 285, 34960-34971 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 34960-34971
    • Jiang, S.1
  • 53
    • 80053338210 scopus 로고    scopus 로고
    • Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: Identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1
    • Jiang, S., Wells, C. D. & Roach, P. J. Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1. Biochem. Biophys. Res. Commun. 413, 420-425 (2011).
    • (2011) Biochem. Biophys. Res. Commun. , vol.413 , pp. 420-425
    • Jiang, S.1    Wells, C.D.2    Roach, P.J.3
  • 54
    • 67650261893 scopus 로고    scopus 로고
    • The values and limits of an in vitro model of Pompe disease: The best laid schemes o' mice an' men
    • Takikita, S. et al. The values and limits of an in vitro model of Pompe disease: the best laid schemes o' mice an' men. Autophagy 5, 729-731 (2009).
    • (2009) Autophagy , vol.5 , pp. 729-731
    • Takikita, S.1
  • 55
    • 79959371914 scopus 로고    scopus 로고
    • Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth
    • Lv, L. et al. Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth. Mol. Cell 42, 719-730 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 719-730
    • Lv, L.1
  • 56
    • 66449099090 scopus 로고    scopus 로고
    • Autophagy suppresses tumorigenesis through elimination of p62
    • Mathew, R. et al. Autophagy suppresses tumorigenesis through elimination of p62. Cell 137, 1062-1075 (2009).
    • (2009) Cell , vol.137 , pp. 1062-1075
    • Mathew, R.1
  • 57
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu, M. et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149-1163 (2007).
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1
  • 58
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig, G. et al. Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J. 27, 433-446 (2008).
    • (2008) EMBO J. , vol.27 , pp. 433-446
    • Twig, G.1
  • 60
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D. F. & Youle, R. J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183, 795-803 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 61
    • 79954571354 scopus 로고    scopus 로고
    • The interplay between mitochondrial dynamics and mitophagy
    • Twig, G. & Shirihai, O. S. The interplay between mitochondrial dynamics and mitophagy. Antioxid. Redox Signal. 14, 1939-1951 (2011).
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1939-1951
    • Twig, G.1    Shirihai, O.S.2
  • 62
    • 37649017266 scopus 로고    scopus 로고
    • NIX is required for programmed mitochondrial clearance during reticulocyte maturation
    • Schweers, R. L. et al. NIX is required for programmed mitochondrial clearance during reticulocyte maturation. Proc. Natl Acad. Sci. USA 104, 19500-19505 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19500-19505
    • Schweers, R.L.1
  • 63
    • 84864015441 scopus 로고    scopus 로고
    • BNip3 regulates mitochondrial function and lipid metabolism in the liver
    • Glick, D. et al. BNip3 regulates mitochondrial function and lipid metabolism in the liver. Mol. Cell. Biol. 32, 2570-2584 (2012).
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2570-2584
    • Glick, D.1
  • 64
    • 84871279726 scopus 로고    scopus 로고
    • Parkin and mitofusins reciprocally regulate mitophagy and mitochondrial spheroid formation
    • Ding, W. X. et al. Parkin and mitofusins reciprocally regulate mitophagy and mitochondrial spheroid formation. J. Biol. Chem. 287, 42379-42388 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 42379-42388
    • Ding, W.X.1
  • 65
    • 79251587803 scopus 로고    scopus 로고
    • Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
    • Egan, D. F. et al. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 331, 456-461 (2011).
    • (2011) Science , vol.331 , pp. 456-461
    • Egan, D.F.1
  • 66
    • 51349095898 scopus 로고    scopus 로고
    • Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
    • Zhang, C. & Cuervo, A. M. Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat. Med. 14, 959-965 (2008).
    • (2008) Nat. Med. , vol.14 , pp. 959-965
    • Zhang, C.1    Cuervo, A.M.2
  • 67
    • 39749148228 scopus 로고    scopus 로고
    • Comprehensive proteomics analysis of autophagy-deficient mouse liver
    • Matsumoto, N. et al. Comprehensive proteomics analysis of autophagy-deficient mouse liver. Biochem. Biophys. Res. Commun. 368, 643-649 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 643-649
    • Matsumoto, N.1
  • 68
    • 77954599053 scopus 로고    scopus 로고
    • P62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • Jain, A. et al. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J. Biol. Chem. 285, 22576-22591 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 22576-22591
    • Jain, A.1
  • 69
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between Keap1 and p62
    • Lau, A. et al. A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62. Mol. Cell. Biol. 30, 3275-3285 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3275-3285
    • Lau, A.1
  • 70
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu, M. et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat. Cell Biol. 12, 213-223 (2010).
    • (2010) Nat. Cell Biol. , vol.12 , pp. 213-223
    • Komatsu, M.1
  • 71
    • 84865287281 scopus 로고    scopus 로고
    • Keap1 degradation by autophagy for the maintenance of redox homeostasis
    • Taguchi, K. et al. Keap1 degradation by autophagy for the maintenance of redox homeostasis. Proc. Natl Acad. Sci. USA 109, 13561-13566 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 13561-13566
    • Taguchi, K.1
  • 72
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval, R. et al. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 26, 1749-1760 (2007).
    • (2007) EMBO J. , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1
  • 73
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • Ogata, M. et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol. Cell. Biol. 26, 9220-9231 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9220-9231
    • Ogata, M.1
  • 74
    • 33749579383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress triggers autophagy
    • Yorimitsu, T., Nair, U., Yang, Z. & Klionsky, D. J. Endoplasmic reticulum stress triggers autophagy. J. Biol. Chem. 281, 30299-30304 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 30299-30304
    • Yorimitsu, T.1    Nair, U.2    Yang, Z.3    Klionsky, D.J.4
  • 75
    • 84856393784 scopus 로고    scopus 로고
    • The transcription factor c-Jun protects against sustained hepatic endoplasmic reticulum stress thereby promoting hepatocyte survival
    • Fuest, M. et al. The transcription factor c-Jun protects against sustained hepatic endoplasmic reticulum stress thereby promoting hepatocyte survival. Hepatology 55, 408-418 (2012).
    • (2012) Hepatology , vol.55 , pp. 408-418
    • Fuest, M.1
  • 76
    • 33846211417 scopus 로고    scopus 로고
    • ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation
    • Kouroku, Y. et al. ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ. 14, 230-239 (2007).
    • (2007) Cell Death Differ. , vol.14 , pp. 230-239
    • Kouroku, Y.1
  • 77
    • 34248581851 scopus 로고    scopus 로고
    • ER-phagy: Selective autophagy of the endoplasmic reticulum
    • Bernales, S., Schuck, S. & Walter, P. ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy 3, 285-287 (2007).
    • (2007) Autophagy , vol.3 , pp. 285-287
    • Bernales, S.1    Schuck, S.2    Walter, P.3
  • 78
    • 77956400005 scopus 로고    scopus 로고
    • Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance
    • Yang, L., Li, P., Fu, S., Calay, E. S. & Hotamisligil, G. S. Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance. Cell Metab. 11, 467-478 (2010).
    • (2010) Cell Metab. , vol.11 , pp. 467-478
    • Yang, L.1    Li, P.2    Fu, S.3    Calay, E.S.4    Hotamisligil, G.S.5
  • 79
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe, E. L. et al. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol. 182, 685-701 (2008).
    • (2008) J. Cell Biol. , vol.182 , pp. 685-701
    • Axe, E.L.1
  • 80
    • 0026755363 scopus 로고
    • The mechanism of Z α1-antitrypsin accumulation in the liver
    • Lomas, D. A., Evans, D. L., Finch, J. T. & Carrell, R. W. The mechanism of Z α1-antitrypsin accumulation in the liver. Nature 357, 605-607 (1992).
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 81
    • 84863975723 scopus 로고    scopus 로고
    • Hepatic fibrosis and carcinogenesis in alpha1-antitrypsin deficiency: A prototype for chronic tissue damage in gain-of-function disorders
    • Perlmutter, D. H. & Silverman, G. A. Hepatic fibrosis and carcinogenesis in alpha1-antitrypsin deficiency: a prototype for chronic tissue damage in gain-of-function disorders. Cold Spring Harb. Perspect. Biol. 3 (2011).
    • Cold Spring Harb. Perspect. Biol. , vol.3 , pp. 2011
    • Perlmutter, D.H.1    Silverman, G.A.2
  • 82
    • 33645216184 scopus 로고    scopus 로고
    • Intracellular inclusions containing mutant α1-antitrypsin Z are propagated in the absence of autophagic activity
    • Kamimoto, T. et al. Intracellular inclusions containing mutant α1-antitrypsin Z are propagated in the absence of autophagic activity. J. Biol. Chem. 281, 4467-4476 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 4467-4476
    • Kamimoto, T.1
  • 83
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • Qu, D., Teckman, J. H., Omura, S. & Perlmutter, D. H. Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271, 22791-22795 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 84
    • 0036840471 scopus 로고    scopus 로고
    • Fasting in alpha1-antitrypsin deficient liver: Consultative activation of autophagy
    • Teckman, J. H., An, J. K., Loethen, S. & Perlmutter, D. H. Fasting in alpha1-antitrypsin deficient liver: consultative activation of autophagy. Am. J. Physiol. 283, G1156-G1165 (2002).
    • (2002) Am. J. Physiol. , vol.283
    • Teckman, J.H.1    An, J.K.2    Loethen, S.3    Perlmutter, D.H.4
  • 85
    • 77954597127 scopus 로고    scopus 로고
    • An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis
    • Hidvegi, T. et al. An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis. Science 329, 229-232 (2010).
    • (2010) Science , vol.329 , pp. 229-232
    • Hidvegi, T.1
  • 86
    • 84895919944 scopus 로고    scopus 로고
    • US National Library of Medicine. ClinicalTrials.gov [online]
    • US National Library of Medicine. ClinicalTrials.gov [online] http://clinicaltrials.gov/show/NCT01379469 (2013).
    • (2013)
  • 87
    • 84874712704 scopus 로고    scopus 로고
    • Gene transfer of master autophagy regulator TFEB results in clearance of toxic protein and correction of hepatic disease in α-1-anti-trypsin deficiency
    • Pastore, N. et al. Gene transfer of master autophagy regulator TFEB results in clearance of toxic protein and correction of hepatic disease in α-1-anti-trypsin deficiency. EMBO Mol. Med. 5, 397-412 (2013).
    • (2013) EMBO Mol. Med. , vol.5 , pp. 397-412
    • Pastore, N.1
  • 88
    • 77954584198 scopus 로고    scopus 로고
    • Autophagy is involved in the elimination of intracellular inclusions, Mallory-Denk bodies, in hepatocytes
    • Harada, M. Autophagy is involved in the elimination of intracellular inclusions, Mallory-Denk bodies, in hepatocytes. Med. Mol. Morphol. 43, 13-18 (2010).
    • (2010) Med. Mol. Morphol. , vol.43 , pp. 13-18
    • Harada, M.1
  • 89
    • 70349829009 scopus 로고    scopus 로고
    • Concurrent induction of necrosis, apoptosis, and autophagy in ischemic preconditioned human livers formerly treated by chemotherapy
    • Domart, M. C. et al. Concurrent induction of necrosis, apoptosis, and autophagy in ischemic preconditioned human livers formerly treated by chemotherapy. J. Hepatol. 51, 881-889 (2009).
    • (2009) J. Hepatol. , vol.51 , pp. 881-889
    • Domart, M.C.1
  • 90
    • 20244373331 scopus 로고    scopus 로고
    • Participation of autophagy in the degeneration process of rat hepatocytes after transplantation following prolonged cold preservation
    • Lu, Z. et al. Participation of autophagy in the degeneration process of rat hepatocytes after transplantation following prolonged cold preservation. Arch. Histol. Cytol. 68, 71-80 (2005).
    • (2005) Arch. Histol. Cytol. , vol.68 , pp. 71-80
    • Lu, Z.1
  • 91
    • 43949096967 scopus 로고    scopus 로고
    • Impaired autophagy: A mechanism of mitochondrial dysfunction in anoxic rat hepatocytes
    • Kim, J. S. et al. Impaired autophagy: a mechanism of mitochondrial dysfunction in anoxic rat hepatocytes. Hepatology 47, 1725-1736 (2008).
    • (2008) Hepatology , vol.47 , pp. 1725-1736
    • Kim, J.S.1
  • 92
    • 65249154907 scopus 로고    scopus 로고
    • Participation of autophagy in the initiation of graft dysfunction after rat liver transplantation
    • Gotoh, K. et al. Participation of autophagy in the initiation of graft dysfunction after rat liver transplantation. Autophagy 5, 351-360 (2009).
    • (2009) Autophagy , vol.5 , pp. 351-360
    • Gotoh, K.1
  • 93
    • 84888395956 scopus 로고    scopus 로고
    • Dual role of chloroquine in liver ischemia reperfusion injury: Reduction of liver damage in early phase, but aggravation in late phase
    • Fang, H., Liu, A., Dahmen, U. & Dirsch, O. Dual role of chloroquine in liver ischemia reperfusion injury: reduction of liver damage in early phase, but aggravation in late phase. Cell Death Dis. 4, e694 (2013).
    • (2013) Cell Death Dis. , vol.4
    • Fang, H.1    Liu, A.2    Dahmen, U.3    Dirsch, O.4
  • 94
    • 84860792150 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system inhibitors and AMPK regulation in hepatic cold ischaemia and reperfusion injury: Possible mechanisms
    • Padrissa-Altes, S., Zaouali, M. A., Bartrons, R. & Rosello-Catafau, J. Ubiquitin-proteasome system inhibitors and AMPK regulation in hepatic cold ischaemia and reperfusion injury: possible mechanisms. Clin. Sci. (Lond.) 123, 93-98 (2012).
    • (2012) Clin. Sci. (Lond.) , vol.123 , pp. 93-98
    • Padrissa-Altes, S.1    Zaouali, M.A.2    Bartrons, R.3    Rosello-Catafau, J.4
  • 95
    • 84885190019 scopus 로고    scopus 로고
    • AMPK involvement in endoplasmic reticulum stress and autophagy modulation after fatty liver graft preservation: A role for melatonin and trimetazidine cocktail
    • Zaouali, M. A. et al. AMPK involvement in endoplasmic reticulum stress and autophagy modulation after fatty liver graft preservation: a role for melatonin and trimetazidine cocktail. J. Pineal. Res. 55, 65-78 (2013).
    • (2013) J. Pineal. Res. , vol.55 , pp. 65-78
    • Zaouali, M.A.1
  • 96
    • 84863889307 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase IV limits organ damage in hepatic ischemia-reperfusion injury through induction of autophagy
    • Evankovich, J. et al. Calcium/calmodulin-dependent protein kinase IV limits organ damage in hepatic ischemia-reperfusion injury through induction of autophagy. Am. J. Physiol. Gastrointest. Liver Physiol. 303, G189-G198 (2012).
    • (2012) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.303
    • Evankovich, J.1
  • 97
    • 84879526538 scopus 로고    scopus 로고
    • Chronic lithium treatment protects against liver ischemia/reperfusion injury in rats
    • Liu, A., Fang, H., Dahmen, U. & Dirsch, O. Chronic lithium treatment protects against liver ischemia/reperfusion injury in rats. Liver Transpl. 19, 762-772 (2013).
    • (2013) Liver Transpl. , vol.19 , pp. 762-772
    • Liu, A.1    Fang, H.2    Dahmen, U.3    Dirsch, O.4
  • 98
    • 79959997977 scopus 로고    scopus 로고
    • Ischemic preconditioning induces autophagy and limits necrosis in human recipients of fatty liver grafts, decreasing the incidence of rejection episodes
    • Degli Esposti, D. et al. Ischemic preconditioning induces autophagy and limits necrosis in human recipients of fatty liver grafts, decreasing the incidence of rejection episodes. Cell Death Dis. 2, e111 (2011).
    • (2011) Cell Death Dis. , vol.2
    • Degli Esposti, D.1
  • 99
    • 81855221944 scopus 로고    scopus 로고
    • Autophagy suppresses age-dependent ischemia and reperfusion injury in livers of mice
    • Wang, J. H. et al. Autophagy suppresses age-dependent ischemia and reperfusion injury in livers of mice. Gastroenterology 141, 2188-2199.e6 (2011).
    • (2011) Gastroenterology , vol.141
    • Wang, J.H.1
  • 100
    • 84864883212 scopus 로고    scopus 로고
    • The role of AKT1 and autophagy in the protective effect of hydrogen sulphide against hepatic ischemia/reperfusion injury in mice
    • Wang, D. et al. The role of AKT1 and autophagy in the protective effect of hydrogen sulphide against hepatic ischemia/reperfusion injury in mice. Autophagy 8, 954-962 (2012).
    • (2012) Autophagy , vol.8 , pp. 954-962
    • Wang, D.1
  • 101
    • 84878694814 scopus 로고    scopus 로고
    • Autophagy lessens ischemic liver injury by reducing oxidative damage
    • Sun, K. et al. Autophagy lessens ischemic liver injury by reducing oxidative damage. Cell Biosci. 3, 26 (2013).
    • (2013) Cell Biosci. , vol.3 , pp. 26
    • Sun, K.1
  • 102
    • 0019961008 scopus 로고
    • Inhibition of hepatocytic protein degradation by inducers of autophagosome accumulation
    • Kovacs, A. L. & Seglen, P. O. Inhibition of hepatocytic protein degradation by inducers of autophagosome accumulation. Acta Biol. Med. Ger. 41, 125-130 (1982).
    • (1982) Acta Biol. Med. Ger. , vol.41 , pp. 125-130
    • Kovacs, A.L.1    Seglen, P.O.2
  • 103
    • 79551554585 scopus 로고    scopus 로고
    • Selective taste of ethanol-induced autophagy for mitochondria and lipid droplets
    • Ding, W. X., Li, M. & Yin, X. M. Selective taste of ethanol-induced autophagy for mitochondria and lipid droplets. Autophagy 7, 248-249 (2011).
    • (2011) Autophagy , vol.7 , pp. 248-249
    • Ding, W.X.1    Li, M.2    Yin, X.M.3
  • 104
    • 80054836991 scopus 로고    scopus 로고
    • Restoration of autophagy by puerarin in ethanol-treated hepatocytes via the activation of AMP-activated protein kinase
    • Noh, B. K. et al. Restoration of autophagy by puerarin in ethanol-treated hepatocytes via the activation of AMP-activated protein kinase. Biochem. Biophys. Res. Commun. 414, 361-366 (2011).
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 361-366
    • Noh, B.K.1
  • 105
    • 84865528809 scopus 로고    scopus 로고
    • Cytochrome P4502E1, oxidative stress, JNK, and autophagy in acute alcohol-induced fatty liver
    • Yang, L., Wu, D., Wang, X. & Cederbaum, A. I. Cytochrome P4502E1, oxidative stress, JNK, and autophagy in acute alcohol-induced fatty liver. Free Radic. Biol. Med. 53, 1170-1180 (2012).
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1170-1180
    • Yang, L.1    Wu, D.2    Wang, X.3    Cederbaum, A.I.4
  • 106
    • 84855779289 scopus 로고    scopus 로고
    • Proteasome activity and autophagosome content in liver are reciprocally regulated by ethanol treatment
    • Thomes, P. G. et al. Proteasome activity and autophagosome content in liver are reciprocally regulated by ethanol treatment. Biochem. Biophys. Res. Commun. 417, 262-267 (2012).
    • (2012) Biochem. Biophys. Res. Commun. , vol.417 , pp. 262-267
    • Thomes, P.G.1
  • 107
    • 84872191827 scopus 로고    scopus 로고
    • Multilevel regulation of autophagosome content by ethanol oxidation in HepG2 cells
    • Thomes, P. G. et al. Multilevel regulation of autophagosome content by ethanol oxidation in HepG2 cells. Autophagy 9, 63-73 (2013).
    • (2013) Autophagy , vol.9 , pp. 63-73
    • Thomes, P.G.1
  • 108
    • 84884905298 scopus 로고    scopus 로고
    • Role of AMPK activation in oxidative cell damage: Implications for alcohol-induced liver disease
    • Sid, B., Verrax, J. & Calderon, P. B. Role of AMPK activation in oxidative cell damage: Implications for alcohol-induced liver disease. Biochem. Pharmacol. 86, 200-209 (2013).
    • (2013) Biochem. Pharmacol. , vol.86 , pp. 200-209
    • Sid, B.1    Verrax, J.2    Calderon, P.B.3
  • 109
    • 78049236043 scopus 로고    scopus 로고
    • CYP2E1 enhances ethanol-induced lipid accumulation but impairs autophagy in HepG2 E47 cells
    • Wu, D., Wang, X., Zhou, R. & Cederbaum, A. CYP2E1 enhances ethanol-induced lipid accumulation but impairs autophagy in HepG2 E47 cells. Biochem. Biophys. Res. Commun. 402, 116-122 (2010).
    • (2010) Biochem. Biophys. Res. Commun. , vol.402 , pp. 116-122
    • Wu, D.1    Wang, X.2    Zhou, R.3    Cederbaum, A.4
  • 110
    • 84155194923 scopus 로고    scopus 로고
    • Activation of autophagy protects against acetaminophen-induced hepatotoxicity
    • Ni, H. M., Bockus, A., Boggess, N., Jaeschke, H. & Ding, W. X. Activation of autophagy protects against acetaminophen-induced hepatotoxicity. Hepatology 55, 222-232 (2012).
    • (2012) Hepatology , vol.55 , pp. 222-232
    • Ni, H.M.1    Bockus, A.2    Boggess, N.3    Jaeschke, H.4    Ding, W.X.5
  • 111
    • 84884530954 scopus 로고    scopus 로고
    • Hepatic energy metabolism in human diabetes mellitus, obesity and non-alcoholic fatty liver disease
    • Koliaki, C. & Roden, M. Hepatic energy metabolism in human diabetes mellitus, obesity and non-alcoholic fatty liver disease. Mol. Cell. Endocrinol. 379, 35-42 (2013).
    • (2013) Mol. Cell. Endocrinol. , vol.379 , pp. 35-42
    • Koliaki, C.1    Roden, M.2
  • 112
    • 84878699998 scopus 로고    scopus 로고
    • Chronic caloric restriction and exercise improve metabolic conditions of dietary-induced obese mice in autophagy correlated manner without involving AMPK
    • Cui, M., Yu, H., Wang, J., Gao, J. & Li, J. Chronic caloric restriction and exercise improve metabolic conditions of dietary-induced obese mice in autophagy correlated manner without involving AMPK. J. Diabetes Res. 2013, 852754 (2013).
    • (2013) J. Diabetes Res. , vol.2013 , pp. 852754
    • Cui, M.1    Yu, H.2    Wang, J.3    Gao, J.4    Li, J.5
  • 113
    • 77955789211 scopus 로고    scopus 로고
    • Altered lipid content inhibits autophagic vesicular fusion
    • Koga, H., Kaushik, S. & Cuervo, A. M. Altered lipid content inhibits autophagic vesicular fusion. FASEB J. 24, 3052-3065 (2010).
    • (2010) FASEB J. , vol.24 , pp. 3052-3065
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 114
    • 71449091240 scopus 로고    scopus 로고
    • Hepatic autophagy is suppressed in the presence of insulin resistance and hyperinsulinemia: Inhibition of FoxO1-dependent expression of key autophagy genes by insulin
    • Liu, H. Y. et al. Hepatic autophagy is suppressed in the presence of insulin resistance and hyperinsulinemia: inhibition of FoxO1-dependent expression of key autophagy genes by insulin. J. Biol. Chem. 284, 31484-31492 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 31484-31492
    • Liu, H.Y.1
  • 115
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo, A. M. & Dice, J. F. Age-related decline in chaperone-mediated autophagy. J. Biol. Chem. 275, 31505-31513 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 116
    • 84858659826 scopus 로고    scopus 로고
    • Inhibitory effect of dietary lipids on chaperone-mediated autophagy
    • Rodriguez-Navarro, J. A. et al. Inhibitory effect of dietary lipids on chaperone-mediated autophagy. Proc. Natl Acad. Sci. USA 109, E705-E714 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109
    • Rodriguez-Navarro, J.A.1
  • 117
    • 84876287362 scopus 로고    scopus 로고
    • Pharmacological promotion of autophagy alleviates steatosis and injury in alcoholic and non-alcoholic fatty liver conditions in mice
    • Lin, C. W. et al. Pharmacological promotion of autophagy alleviates steatosis and injury in alcoholic and non-alcoholic fatty liver conditions in mice. J. Hepatol. 58, 993-999 (2013).
    • (2013) J. Hepatol. , vol.58 , pp. 993-999
    • Lin, C.W.1
  • 118
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine, B., Mizushima, N. & Virgin, H. W. Autophagy in immunity and inflammation. Nature 469, 323-335 (2011).
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 119
    • 79951910694 scopus 로고    scopus 로고
    • Autophagy in immunity and cell-autonomous defense against intracellular microbes
    • Deretic, V. Autophagy in immunity and cell-autonomous defense against intracellular microbes. Immunol. Rev. 240, 92-104 (2011).
    • (2011) Immunol. Rev. , vol.240 , pp. 92-104
    • Deretic, V.1
  • 120
    • 73849087396 scopus 로고    scopus 로고
    • Autophagy in viral replication and pathogenesis
    • Sir, D. & Ou, J. H. Autophagy in viral replication and pathogenesis. Mol. Cells 29, 1-7 (2010).
    • (2010) Mol. Cells , vol.29 , pp. 1-7
    • Sir, D.1    Ou, J.H.2
  • 121
    • 33947715151 scopus 로고    scopus 로고
    • HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein
    • Orvedahl, A. et al. HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein. Cell Host Microbe 1, 23-35 (2007).
    • (2007) Cell Host Microbe , vol.1 , pp. 23-35
    • Orvedahl, A.1
  • 122
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • Kyei, G. B. et al. Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages. J. Cell. Biol. 186, 255-268 (2009).
    • (2009) J. Cell. Biol. , vol.186 , pp. 255-268
    • Kyei, G.B.1
  • 124
    • 78049486018 scopus 로고    scopus 로고
    • Autophagy in liver diseases
    • Rautou, P. E. et al. Autophagy in liver diseases. J. Hepatol. 53, 1123-1134 (2010).
    • (2010) J. Hepatol. , vol.53 , pp. 1123-1134
    • Rautou, P.E.1
  • 125
    • 77749292148 scopus 로고    scopus 로고
    • The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication
    • Sir, D. et al. The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication. Proc. Natl Acad. Sci. USA 107, 4383-4388 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4383-4388
    • Sir, D.1
  • 126
    • 80052045217 scopus 로고    scopus 로고
    • Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment
    • Li, J. et al. Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment. J. Virol. 85, 6319-6333 (2011).
    • (2011) J. Virol. , vol.85 , pp. 6319-6333
    • Li, J.1
  • 127
    • 84855824374 scopus 로고    scopus 로고
    • Autophagy required for hepatitis B virus replication in transgenic mice
    • Tian, Y., Sir, D., Kuo, C. F., Ann, D. K. & Ou, J. H. Autophagy required for hepatitis B virus replication in transgenic mice. J. Virol. 85, 13453-13456 (2011).
    • (2011) J. Virol. , vol.85 , pp. 13453-13456
    • Tian, Y.1    Sir, D.2    Kuo, C.F.3    Ann, D.K.4    Ou, J.H.5
  • 128
    • 58949098335 scopus 로고    scopus 로고
    • Hepatitis B virus X protein sensitizes cells to starvation-induced autophagy via up-regulation of beclin 1 expression
    • Tang, H. et al. Hepatitis B virus X protein sensitizes cells to starvation-induced autophagy via up-regulation of beclin 1 expression. Hepatology 49, 60-71 (2009).
    • (2009) Hepatology , vol.49 , pp. 60-71
    • Tang, H.1
  • 129
    • 79959478969 scopus 로고    scopus 로고
    • Clinical practice. Chronic hepatitis C infection
    • Rosen, H. R. Clinical practice. Chronic hepatitis C infection. N. Engl. J. Med. 364, 2429-2438 (2011).
    • (2011) N. Engl. J. Med. , vol.364 , pp. 2429-2438
    • Rosen, H.R.1
  • 130
    • 39749116856 scopus 로고    scopus 로고
    • Hepatitis C virus genotype 1a growth and induction of autophagy
    • Ait-Goughoulte, M. et al. Hepatitis C virus genotype 1a growth and induction of autophagy. J. Virol. 82, 2241-2249 (2008).
    • (2008) J. Virol. , vol.82 , pp. 2241-2249
    • Ait-Goughoulte, M.1
  • 131
    • 69549135689 scopus 로고    scopus 로고
    • The autophagy machinery is required to initiate hepatitis C virus replication
    • Dreux, M., Gastaminza, P., Wieland, S. F. & Chisari, F. V. The autophagy machinery is required to initiate hepatitis C virus replication. Proc. Natl Acad. Sci. USA 106, 14046-14051 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14046-14051
    • Dreux, M.1    Gastaminza, P.2    Wieland, S.F.3    Chisari, F.V.4
  • 132
    • 54449101892 scopus 로고    scopus 로고
    • Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response
    • Sir, D. et al. Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response. Hepatology 48, 1054-1061 (2008).
    • (2008) Hepatology , vol.48 , pp. 1054-1061
    • Sir, D.1
  • 133
    • 80054978956 scopus 로고    scopus 로고
    • Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy
    • Su, W. C. et al. Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy. J. Virol. 85, 10561-10571 (2011).
    • (2011) J. Virol. , vol.85 , pp. 10561-10571
    • Su, W.C.1
  • 134
    • 84865103087 scopus 로고    scopus 로고
    • Hepatitis C virus upregulates Beclin1 for induction of autophagy and activates mTOR signaling
    • Shrivastava, S., Bhanja Chowdhury, J., Steele, R., Ray, R. & Ray, R. B. Hepatitis C virus upregulates Beclin1 for induction of autophagy and activates mTOR signaling. J. Virol. 86, 8705-8712 (2012).
    • (2012) J. Virol. , vol.86 , pp. 8705-8712
    • Shrivastava, S.1    Bhanja Chowdhury, J.2    Steele, R.3    Ray, R.4    Ray, R.B.5
  • 135
    • 84875993938 scopus 로고    scopus 로고
    • Hepatitis C virus induces the mitochondrial translocation of Parkin and subsequent mitophagy
    • Kim, S. J., Syed, G. H. & Siddiqui, A. Hepatitis C virus induces the mitochondrial translocation of Parkin and subsequent mitophagy. PLoS Pathog. 9, e1003285 (2013).
    • (2013) PLoS Pathog. , vol.9
    • Kim, S.J.1    Syed, G.H.2    Siddiqui, A.3
  • 136
    • 78650961487 scopus 로고    scopus 로고
    • Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro
    • Ke, P. Y. & Chen, S. S. Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro. J. Clin. Invest. 121, 37-56 (2011).
    • (2011) J. Clin. Invest. , vol.121 , pp. 37-56
    • Ke, P.Y.1    Chen, S.S.2
  • 137
    • 84855827121 scopus 로고    scopus 로고
    • Dysfunction of autophagy participates in vacuole formation and cell death in cells replicating hepatitis C virus
    • Taguwa, S. et al. Dysfunction of autophagy participates in vacuole formation and cell death in cells replicating hepatitis C virus. J. Virol. 85, 13185-13194 (2011).
    • (2011) J. Virol. , vol.85 , pp. 13185-13194
    • Taguwa, S.1
  • 138
    • 0345144016 scopus 로고    scopus 로고
    • Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons
    • Gosert, R. et al. Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons. J. Virol. 77, 5487-5492 (2003).
    • (2003) J. Virol. , vol.77 , pp. 5487-5492
    • Gosert, R.1
  • 139
    • 77955515860 scopus 로고    scopus 로고
    • Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection
    • Guevin, C. et al. Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection. Virology 405, 1-7 (2010).
    • (2010) Virology , vol.405 , pp. 1-7
    • Guevin, C.1
  • 140
    • 67349268146 scopus 로고    scopus 로고
    • Lipid droplets and hepatitis C virus infection
    • McLauchlan, J. Lipid droplets and hepatitis C virus infection. Biochim. Biophys. Acta 1791, 552-559 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 552-559
    • McLauchlan, J.1
  • 141
    • 79251512287 scopus 로고    scopus 로고
    • Knockdown of autophagy enhances the innate immune response in hepatitis C virus-infected hepatocytes
    • Shrivastava, S., Raychoudhuri, A., Steele, R., Ray, R. & Ray, R. B. Knockdown of autophagy enhances the innate immune response in hepatitis C virus-infected hepatocytes. Hepatology 53, 406-414 (2011).
    • (2011) Hepatology , vol.53 , pp. 406-414
    • Shrivastava, S.1    Raychoudhuri, A.2    Steele, R.3    Ray, R.4    Ray, R.B.5
  • 142
    • 0027787534 scopus 로고
    • Reduced autophagic activity in primary rat hepatocellular carcinoma and ascites hepatoma cells
    • Kisen, G. O. et al. Reduced autophagic activity in primary rat hepatocellular carcinoma and ascites hepatoma cells. Carcinogenesis 14, 2501-2505 (1993).
    • (1993) Carcinogenesis , vol.14 , pp. 2501-2505
    • Kisen, G.O.1
  • 143
    • 34249863298 scopus 로고    scopus 로고
    • Autophagy suppresses tumor progression by limiting chromosomal instability
    • Mathew, R. et al. Autophagy suppresses tumor progression by limiting chromosomal instability. Genes Dev. 21, 1367-1381 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1367-1381
    • Mathew, R.1
  • 144
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • Liang, X. et al. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 402, 672-676 (1999).
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.1
  • 145
    • 79960097021 scopus 로고    scopus 로고
    • Role of autophagy in cancer prevention
    • Chen, H. Y. & White, E. Role of autophagy in cancer prevention. Cancer Prev. Res. (Phila.) 4, 973-983 (2011).
    • (2011) Cancer Prev. Res. (Phila.) , vol.4 , pp. 973-983
    • Chen, H.Y.1    White, E.2
  • 146
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B. & Kroemer, G. Autophagy in the pathogenesis of disease. Cell 132, 27-42 (2008).
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 147
    • 84861526009 scopus 로고    scopus 로고
    • Deconvoluting the context-dependent role for autophagy in cancer
    • White, E. Deconvoluting the context-dependent role for autophagy in cancer. Nat. Rev. Cancer 12, 401-410 (2012).
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 401-410
    • White, E.1
  • 148
    • 69349087479 scopus 로고    scopus 로고
    • Anti-and pro-tumor functions of autophagy
    • Morselli, E. et al. Anti-and pro-tumor functions of autophagy. Biochim. Biophys. Acta 1793, 1524-1532 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1524-1532
    • Morselli, E.1
  • 149
    • 0018714307 scopus 로고
    • Inhibited autophagic degradation of cytoplasm during compensatory growth of liver cells after partial hepatectomy
    • Pfeifer, U. Inhibited autophagic degradation of cytoplasm during compensatory growth of liver cells after partial hepatectomy. Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. 30, 313-333 (1979).
    • (1979) Virchows Arch. B Cell Pathol. Incl. Mol. Pathol. , vol.30 , pp. 313-333
    • Pfeifer, U.1
  • 150
    • 80054978627 scopus 로고    scopus 로고
    • Autophagy in hypoxia protects cancer cells against apoptosis induced by nutrient deprivation through a Beclin1-dependent way in hepatocellular carcinoma
    • Song, J. et al. Autophagy in hypoxia protects cancer cells against apoptosis induced by nutrient deprivation through a Beclin1-dependent way in hepatocellular carcinoma. J. Cell. Biochem. 112, 3406-3420 (2011).
    • (2011) J. Cell. Biochem. , vol.112 , pp. 3406-3420
    • Song, J.1
  • 151
    • 79955377420 scopus 로고    scopus 로고
    • Autophagy-deficient mice develop multiple liver tumors
    • Takamura, A. et al. Autophagy-deficient mice develop multiple liver tumors. Genes Dev. 25, 795-800 (2011).
    • (2011) Genes Dev. , vol.25 , pp. 795-800
    • Takamura, A.1
  • 152
    • 56449107131 scopus 로고    scopus 로고
    • Association of autophagy defect with a malignant phenotype and poor prognosis of hepatocellular carcinoma
    • Ding, Z. B. et al. Association of autophagy defect with a malignant phenotype and poor prognosis of hepatocellular carcinoma. Cancer Res. 68, 9167-9175 (2008).
    • (2008) Cancer Res. , vol.68 , pp. 9167-9175
    • Ding, Z.B.1
  • 153
    • 9144240441 scopus 로고    scopus 로고
    • Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
    • Qu, X. 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
  • 154
    • 84901405852 scopus 로고    scopus 로고
    • Autophagy enhances hepatocellular carcinoma progression by activation of mitochondrial beta-oxidation
    • Toshima, T. et al. Autophagy enhances hepatocellular carcinoma progression by activation of mitochondrial beta-oxidation. J. Gastroenterol. http://dx.doi.org/10.1007/s00535-013-0835-0.
    • J. Gastroenterol
    • Toshima, T.1
  • 155
    • 84878997506 scopus 로고    scopus 로고
    • Autophagy promotes hepatocellular carcinoma cell invasion through activation of epithelial-mesenchymal transition
    • Li, J. et al. Autophagy promotes hepatocellular carcinoma cell invasion through activation of epithelial-mesenchymal transition. Carcinogenesis 34, 1343-1351 (2013).
    • (2013) Carcinogenesis , vol.34 , pp. 1343-1351
    • Li, J.1
  • 156
    • 77950500675 scopus 로고    scopus 로고
    • Autophagy in cellular growth control
    • Wang, R. C. & Levine, B. Autophagy in cellular growth control. FEBS Lett. 584, 1417-1426 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 1417-1426
    • Wang, R.C.1    Levine, B.2
  • 157
    • 79955492012 scopus 로고    scopus 로고
    • Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells
    • Inami, Y. et al. Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells. J. Cell. Biol. 193, 275-284 (2011).
    • (2011) J. Cell. Biol. , vol.193 , pp. 275-284
    • Inami, Y.1
  • 158
    • 80053420059 scopus 로고    scopus 로고
    • Targeting autophagy enhances sorafenib lethality for hepatocellular carcinoma via ER stress-related apoptosis
    • Shi, Y. H. et al. Targeting autophagy enhances sorafenib lethality for hepatocellular carcinoma via ER stress-related apoptosis. Autophagy 7, 1159-1172 (2011).
    • (2011) Autophagy , vol.7 , pp. 1159-1172
    • Shi, Y.H.1
  • 159
    • 84873949249 scopus 로고    scopus 로고
    • Role of sorafenib in the treatment of advanced hepatocellular carcinoma: An update
    • Gauthier, A. & Ho, M. Role of sorafenib in the treatment of advanced hepatocellular carcinoma: An update. Hepatol. Res. 43, 147-154 (2013).
    • (2013) Hepatol. Res. , vol.43 , pp. 147-154
    • Gauthier, A.1    Ho, M.2
  • 160
    • 84879605085 scopus 로고    scopus 로고
    • Inhibition of autophagy enhances anticancer effects of bevacizumab in hepatocarcinoma
    • Guo, X. L. et al. Inhibition of autophagy enhances anticancer effects of bevacizumab in hepatocarcinoma. J. Mol. Med. (Berl.) 91, 473-483 (2013).
    • (2013) J. Mol. Med. (Berl.) , vol.91 , pp. 473-483
    • Guo, X.L.1
  • 161
    • 78649299438 scopus 로고    scopus 로고
    • Autophagy potentiates the anti-cancer effects of the histone deacetylase inhibitors in hepatocellular carcinoma
    • Liu, Y. L. et al. Autophagy potentiates the anti-cancer effects of the histone deacetylase inhibitors in hepatocellular carcinoma. Autophagy 6, 1057-1065 (2010).
    • (2010) Autophagy , vol.6 , pp. 1057-1065
    • Liu, Y.L.1
  • 162
    • 84861344950 scopus 로고    scopus 로고
    • Phase II study of sirolimus in treatment-naive patients with advanced hepatocellular carcinoma
    • Decaens, T. et al. Phase II study of sirolimus in treatment-naive patients with advanced hepatocellular carcinoma. Dig. Liver Dis. 44, 610-616 (2012).
    • (2012) Dig. Liver Dis. , vol.44 , pp. 610-616
    • Decaens, T.1
  • 163
    • 84876211114 scopus 로고    scopus 로고
    • MiR-101 inhibits autophagy and enhances cisplatin-induced apoptosis in hepatocellular carcinoma cells
    • Xu, Y. et al. miR-101 inhibits autophagy and enhances cisplatin-induced apoptosis in hepatocellular carcinoma cells. Oncol. Rep. 29, 2019-2024 (2013).
    • (2013) Oncol. Rep. , vol.29 , pp. 2019-2024
    • Xu, Y.1
  • 164
    • 81455128769 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy is required for tumor growth
    • Kon, M. et al. Chaperone-mediated autophagy is required for tumor growth. Sci. Transl. Med. 3, ra117 (2011).
    • (2011) Sci. Transl. Med. , vol.3
    • Kon, M.1
  • 165
    • 84869428389 scopus 로고    scopus 로고
    • LAMP2A overexpression in breast tumors promotes cancer cell survival via chaperone-mediated autophagy
    • Saha, T. LAMP2A overexpression in breast tumors promotes cancer cell survival via chaperone-mediated autophagy. Autophagy 8 (2012).
    • (2012) Autophagy , vol.8
    • Saha, T.1


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