메뉴 건너뛰기




Volumn 152, Issue 1, 2012, Pages 5-15

Liver autophagy: Physiology and pathology

Author keywords

Atg; autophagy; hepatic tumour; liver; p62

Indexed keywords

ATG GENE; AUTOPHAGOSOME; AUTOPHAGY; CARCINOGENESIS; GENE; KNOCKOUT MOUSE; LIVER DISEASE; LYSOSOME; NONHUMAN; REVIEW;

EID: 84863710652     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvs059     Document Type: Review
Times cited : (54)

References (81)
  • 1
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., Levine, B., Cuervo, A.M., and Klionsky, D.J. (2008) Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 2
  • 3
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • Xie, Z. and Klionsky, D.J. (2007) Autophagosome formation: core machinery and adaptations. Nat. Cell. Biol. 9, 1102-1109
    • (2007) Nat. Cell. Biol. , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 8
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim, J., Kundu, M., Viollet, B., and Guan, K.L. (2011) AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell. Biol. 13, 132-141
    • (2011) Nat. Cell. Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 10
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • Itakura, E. and Mizushima, N. (2010) Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy 6, 764-776
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 12
    • 33745751085 scopus 로고    scopus 로고
    • Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
    • Liang, C., Feng, P., Ku, B., Dotan, I., Canaani, D., Oh, B.H., and Jung, J.U. (2006) Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG. Nat. Cell. Biol. 8, 688-699
    • (2006) Nat. Cell. Biol. , vol.8 , pp. 688-699
    • Liang, C.1    Feng, P.2    Ku, B.3    Dotan, I.4    Canaani, D.5    Oh, B.H.6    Jung, J.U.7
  • 15
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • Zhong, Y., Wang, Q.J., Li, X., Yan, Y., Backer, J.M., Chait, B.T., Heintz, N., and Yue, Z. (2009) Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat. Cell. Biol. 11, 468-476
    • (2009) Nat. Cell. Biol. , vol.11 , pp. 468-476
    • Zhong, Y.1    Wang, Q.J.2    Li, X.3    Yan, Y.4    Backer, J.M.5    Chait, B.T.6    Heintz, N.7    Yue, Z.8
  • 16
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • Wei, Y., Pattingre, S., Sinha, S., Bassik, M., and Levine, B. (2008) JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol. Cell. 30, 678-688
    • (2008) Mol. Cell. , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 17
    • 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., Walker, S.A., Manifava, M., Chandra, P., Roderick, H.L., Habermann, A., Griffiths, G., and Ktistakis, N.T. (2008) Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol 182, 685-701
    • (2008) J. Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 18
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasomeanchored phagophores and positively regulates LC3 lipidation
    • Polson, H.E., de Lartigue, J., Rigden, D.J., Reedijk, M., Urbe, S., Clague, M.J., and Tooze, S.A. (2010) Mammalian Atg18 (WIPI2) localizes to omegasomeanchored phagophores and positively regulates LC3 lipidation. Autophagy 6, 506-522
    • (2010) Autophagy , vol.6 , pp. 506-522
    • Polson, H.E.1    De Lartigue, J.2    Rigden, D.J.3    Reedijk, M.4    Urbe, S.5    Clague, M.J.6    Tooze, S.A.7
  • 20
    • 75649085703 scopus 로고    scopus 로고
    • Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and p38IP
    • Webber, J.L. and Tooze, S.A. (2010) Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and p38IP. Embo. J. 29, 27-40
    • (2010) Embo. J. , vol.29 , pp. 27-40
    • Webber, J.L.1    Tooze, S.A.2
  • 21
    • 84861158462 scopus 로고    scopus 로고
    • Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, is required for autophagy
    • Orsi, A., Razi, M., Dooley, H., Robinson, D., Weston, A., Collinson, L., and Tooze, S. (2012) Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, is required for autophagy. Mol. Biol. Cell. 23(10), 1860-1873
    • (2012) Mol. Biol. Cell. , vol.23 , Issue.10 , pp. 1860-1873
    • Orsi, A.1    Razi, M.2    Dooley, H.3    Robinson, D.4    Weston, A.5    Collinson, L.6    Tooze, S.7
  • 25
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita, N., Itoh, T., Omori, H., Fukuda, M., Noda, T., and Yoshimori, T. (2008) The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell. 19, 2092-2100
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 30
    • 77049229661 scopus 로고
    • Tissue fractionation studies.6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • De Duve, C., Pressman, B.C., Gianetto, R., Wattiaux, R., and Appelmans, F. (1955) Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem. J. 60, 604-617
    • (1955) Biochem. J. , vol.60 , pp. 604-617
    • De Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 31
    • 0000730374 scopus 로고
    • Cytoplasmic components in hepatic cell lysosomes
    • Ashford, T.P. and Porter, K.R. (1962) Cytoplasmic components in hepatic cell lysosomes. J. Cell Biol 12, 198-202
    • (1962) J. Cell Biol , vol.12 , pp. 198-202
    • Ashford, T.P.1    Porter, K.R.2
  • 32
    • 0038208502 scopus 로고
    • Cytolysomes and mitochondrial degeneration
    • Novikoff, A.B. and Essner, E. (1962) Cytolysomes and mitochondrial degeneration. J. Cell Biol 15, 140-146
    • (1962) J. Cell Biol , vol.15 , pp. 140-146
    • Novikoff, A.B.1    Essner, E.2
  • 33
    • 0017697151 scopus 로고
    • Induction of autophagy by amino-acid deprivation in perfused rat liver
    • Mortimore, G.E. and Schworer, C.M. (1977) Induction of autophagy by amino-acid deprivation in perfused rat liver. Nature 270, 174-176
    • (1977) Nature , vol.270 , pp. 174-176
    • Mortimore, G.E.1    Schworer, C.M.2
  • 34
    • 0018746575 scopus 로고
    • Glucagon-induced autophagy and proteolysis in rat liver: Mediation by selective deprivation of intracellular amino acids
    • Schworer, C.M. and Mortimore, G.E. (1979) Glucagon-induced autophagy and proteolysis in rat liver: mediation by selective deprivation of intracellular amino acids. Proc. Natl. Acad. Sci. USA. 76, 3169-3173
    • (1979) Proc. Natl. Acad. Sci. USA. , vol.76 , pp. 3169-3173
    • Schworer, C.M.1    Mortimore, G.E.2
  • 35
    • 0018927246 scopus 로고
    • Amino acid inhibition of the autophagic/lysosomal pathway of protein degradation in isolated rat hepatocytes
    • Seglen, P.O., Gordon, P.B., and Poli, A. (1980) Amino acid inhibition of the autophagic/lysosomal pathway of protein degradation in isolated rat hepatocytes. Biochim. Biophys. Acta. 630, 103-118
    • (1980) Biochim. Biophys. Acta. , vol.630 , pp. 103-118
    • Seglen, P.O.1    Gordon, P.B.2    Poli, A.3
  • 36
    • 0005677775 scopus 로고
    • 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen, P.O. and Gordon, P.B. (1982) 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc. Natl. Acad. Sci. USA. 79, 1889-1892
    • (1982) Proc. Natl. Acad. Sci. USA. , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 37
    • 0020510501 scopus 로고
    • Quantitative correlation between proteolysis and macro-and microautophagy in mouse hepatocytes during starvation and refeeding
    • Mortimore, G.E., Hutson, N.J., and Surmacz, C.A. (1983) Quantitative correlation between proteolysis and macro-and microautophagy in mouse hepatocytes during starvation and refeeding. Proc. Natl. Acad. Sci. USA. 80, 2179-2183
    • (1983) Proc. Natl. Acad. Sci. USA. , vol.80 , pp. 2179-2183
    • Mortimore, G.E.1    Hutson, N.J.2    Surmacz, C.A.3
  • 44
    • 51349095898 scopus 로고    scopus 로고
    • Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
    • Zhang, C. and Cuervo, A.M. (2008) Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat. Med. 14, 959-965
    • (2008) Nat. Med. , vol.14 , pp. 959-965
    • Zhang, C.1    Cuervo, A.M.2
  • 46
    • 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., and Hotamisligil, G.S. (2010) Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance. Cell. Metab. 11, 467-478
    • (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
  • 48
    • 46249115957 scopus 로고    scopus 로고
    • Autophagy activation by rapamycin eliminates mouse Mallory-Denk bodies and blocks their proteasome inhibitor-mediated formation
    • Harada, M., Hanada, S., Toivola, D.M., Ghori, N., and Omary, M.B. (2008) Autophagy activation by rapamycin eliminates mouse Mallory-Denk bodies and blocks their proteasome inhibitor-mediated formation. Hepatology 47, 2026-2035
    • (2008) Hepatology , vol.47 , pp. 2026-2035
    • Harada, M.1    Hanada, S.2    Toivola, D.M.3    Ghori, N.4    Omary, M.B.5
  • 50
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway
    • Arico, S., Petiot, A., Bauvy, C., Dubbelhuis, P.F., Meijer, A.J., Codogno, P., and Ogier-Denis, E. (2001) The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway. J. Biol. Chem. 276, 35243-35246
    • (2001) J. Biol. Chem. , vol.276 , pp. 35243-35246
    • Arico, S.1    Petiot, A.2    Bauvy, C.3    Dubbelhuis, P.F.4    Meijer, A.J.5    Codogno, P.6    Ogier-Denis, E.7
  • 54
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • Yue, Z., Jin, S., Yang, C., Levine, A.J., and Heintz, N. (2003) Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc. Natl. Acad. Sci. USA. 100, 15077-15082
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 15077-15082
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 56
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., and Yamamoto, M. (2000) Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J. Biol. Chem. 275, 16023-16029
    • (2000) J. Biol. Chem. , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6    Bannai, S.7    Yamamoto, M.8
  • 57
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen, T. and Lamark, T. (2011) Selective autophagy mediated by autophagic adapter proteins. Autophagy 7, 279-296
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 58
    • 77749301510 scopus 로고    scopus 로고
    • Recent advances in understanding the molecular basis of Paget disease of bone
    • Goode, A. and Layfield, R. (2010) Recent advances in understanding the molecular basis of Paget disease of bone. J. Clin. Pathol. 63, 199-203
    • (2010) J. Clin. Pathol. , vol.63 , pp. 199-203
    • Goode, A.1    Layfield, R.2
  • 59
    • 78651282673 scopus 로고    scopus 로고
    • P62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding
    • Itakura, E. and Mizushima, N. (2011) p62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding. J. Cell Biol 192, 17-27
    • (2011) J. Cell Biol , vol.192 , pp. 17-27
    • Itakura, E.1    Mizushima, N.2
  • 62
    • 79959415069 scopus 로고    scopus 로고
    • Biogenesis and cargo selectivity of autophagosomes
    • Weidberg, H., Shvets, E., and Elazar, Z. (2011) Biogenesis and cargo selectivity of autophagosomes. Annu. Rev. Biochem. 80, 125-156
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 125-156
    • Weidberg, H.1    Shvets, E.2    Elazar, Z.3
  • 63
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D.G., Novak, I., and Dikic, I. (2009) A role for ubiquitin in selective autophagy. Mol. Cell. 34, 259-269
    • (2009) Mol. Cell. , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 65
    • 41549151641 scopus 로고    scopus 로고
    • Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain
    • Nezis, I.P., Simonsen, A., Sagona, A.P., Finley, K., Gaumer, S., Contamine, D., Rusten, T.E., Stenmark, H., and Brech, A. (2008) Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain. J. Cell Biol 180, 1065-1071
    • (2008) J. Cell Biol , vol.180 , pp. 1065-1071
    • Nezis, I.P.1    Simonsen, A.2    Sagona, A.P.3    Finley, K.4    Gaumer, S.5    Contamine, D.6    Rusten, T.E.7    Stenmark, H.8    Brech, A.9
  • 68
    • 0034328882 scopus 로고    scopus 로고
    • The atypical protein kinase Cs. Functional specificity mediated by specific protein adapters
    • Moscat, J. and Diaz-Meco, M.T. (2000) The atypical protein kinase Cs. Functional specificity mediated by specific protein adapters. EMBO. Rep. 1, 399-403
    • (2000) EMBO. Rep. , vol.1 , pp. 399-403
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 69
    • 33846692198 scopus 로고    scopus 로고
    • Signal integration and diversification through the p62 scaffold protein
    • Moscat, J., Diaz-Meco, M.T., and Wooten, M.W. (2007) Signal integration and diversification through the p62 scaffold protein. Trends Biochem. Sci. 32, 95-100
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 95-100
    • Moscat, J.1    Diaz-Meco, M.T.2    Wooten, M.W.3
  • 70
    • 65549085701 scopus 로고    scopus 로고
    • Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling
    • Jin, Z., Li, Y., Pitti, R., Lawrence, D., Pham, V.C., Lill, J.R., and Ashkenazi, A. (2009) Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling. Cell 137, 721-735
    • (2009) Cell , vol.137 , pp. 721-735
    • Jin, Z.1    Li, Y.2    Pitti, R.3    Lawrence, D.4    Pham, V.C.5    Lill, J.R.6    Ashkenazi, A.7
  • 72
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between Keap1 and p62
    • Lau, A., Wang, X.J., Zhao, F., Villeneuve, N.F., Wu, T., Jiang, T., Sun, Z., White, E., and Zhang, D.D. (2010) A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62. Mol. Cell. Biol. 30, 3275-3285
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3275-3285
    • Lau, A.1    Wang, X.J.2    Zhao, F.3    Villeneuve, N.F.4    Wu, T.5    Jiang, T.6    Sun, Z.7    White, E.8    Zhang, D.D.9
  • 73
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • Mizushima, N. and Komatsu, M. (2011) Autophagy: renovation of cells and tissues. Cell 147, 728-741
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 77
    • 78751703950 scopus 로고    scopus 로고
    • Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution
    • Taguchi, K., Motohashi, H., and Yamamoto, M. (2011) Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution. Genes Cells 16, 123-140
    • (2011) Genes Cells , vol.16 , pp. 123-140
    • Taguchi, K.1    Motohashi, H.2    Yamamoto, M.3
  • 78
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer
    • Hayes, J.D. and McMahon, M. (2009) NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer. Trends Biochem. Sci. 34, 176-188
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 80
    • 80054724249 scopus 로고    scopus 로고
    • Succination of Keap1 and activation of Nrf2-dependent antioxidant pathways in FH-deficient papillary renal cell carcinoma type 2
    • Kinch, L., Grishin, N.V., and Brugarolas, J. (2011) Succination of Keap1 and activation of Nrf2-dependent antioxidant pathways in FH-deficient papillary renal cell carcinoma type 2. Cancer Cell 20, 418-420
    • (2011) Cancer Cell , vol.20 , pp. 418-420
    • Kinch, L.1    Grishin, N.V.2    Brugarolas, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.