메뉴 건너뛰기




Volumn 452, Issue 3, 2013, Pages 381-390

Aggrephagy: Lessons from C. elegans

Author keywords

Aggrephagy; Atg gene; Autophagosome; Autophagy; Caenorhabditis elegans; Epg gene

Indexed keywords

ATG1 KINASE COMPLEX; AUTOPHAGY PROTEIN 18; AUTOPHAGY PROTEIN 2; AUTOPHAGY PROTEIN 5; AUTOPHAGY PROTEIN 9; CELL PROTEIN; COATOMER PROTEIN 1; HUNTINGTIN; PROTEIN SERINE THREONINE KINASE VPS15; SEQUESTOSOME 1; UNCLASSIFIED DRUG;

EID: 84878421591     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121721     Document Type: Review
Times cited : (25)

References (99)
  • 1
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • Klionsky, D. J. (2007) Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 8, 931-937
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 2
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • DOI 10.1038/ncb1007-1102, PII NCB1007-1102
    • Xie, Z. and Klionsky, D. J. (2007) Autophagosome formation: core machinery and adaptations. Nat. Cell Biol. 9, 1102-1109 (Pubitemid 47500484)
    • (2007) Nature Cell Biology , vol.9 , Issue.10 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 3
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: Lessons from yeast
    • Nakatogawa, H., Suzuki, K., Kamada, Y. and Ohsumi, Y. (2009) Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat. Rev. Mol. Cell Biol. 10, 931-937
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 931-937
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 4
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B. and Kroemer, G. (2008) Autophagy in the pathogenesis of disease. Cell 132, 27-42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 5
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic, V. and Levine, B. (2009) Autophagy, immunity, and microbial adaptations. Cell Host Microbe 5, 527-549
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 6
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • Mizushima, N. (2007) Autophagy: process and function. Genes Dev. 21, 2861-2873
    • (2007) Genes Dev. , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 7
    • 0009701497 scopus 로고
    • Mechanism of cellular autophagy
    • Dingle, J. T. and Fell, H. B., eds, . North Holland, Amsterdam
    • Ericsson, J. L. (1969) Mechanism of cellular autophagy. In Lysosomes in Biology and Pathology, vol. 2 (Dingle, J. T. and Fell, H. B., eds), pp. 345-395, North Holland, Amsterdam
    • (1969) Lysosomes in Biology and Pathology , vol.2 , pp. 345-395
    • Ericsson, J.L.1
  • 8
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • DOI 10.1016/0014-5793(93)80398-E
    • Tsukada, M. and Ohsumi, Y. (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333, 169-174 (Pubitemid 23306962)
    • (1993) FEBS Letters , vol.333 , Issue.1-2 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 9
    • 0028800171 scopus 로고
    • Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
    • Harding, T. M., Morano, K. A., Scott, S. V. and Klionsky, D. J. (1995) Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J. Cell Biol. 131, 591-602
    • (1995) J. Cell Biol. , vol.131 , pp. 591-602
    • Harding, T.M.1    Morano, K.A.2    Scott, S.V.3    Klionsky, D.J.4
  • 10
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige, K., Baba, M., Tsuboi, S., Noda, T. and Ohsumi, Y. (1992) Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 119, 301-311
    • (1992) J. Cell Biol. , vol.119 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 11
    • 70349919804 scopus 로고    scopus 로고
    • Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes
    • Simonsen, A. and Tooze, S. A. (2009) Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes. J. Cell Biol. 186, 773-782
    • (2009) J. Cell Biol. , vol.186 , pp. 773-782
    • Simonsen, A.1    Tooze, S.A.2
  • 12
    • 67549139908 scopus 로고    scopus 로고
    • Vesicular trafficking and autophagosome formation
    • Longatti, A. and Tooze, S. A. (2009) Vesicular trafficking and autophagosome formation. Cell Death Differ. 16, 956-965
    • (2009) Cell Death Differ. , vol.16 , pp. 956-965
    • Longatti, A.1    Tooze, S.A.2
  • 13
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • DOI 10.1242/jcs.01114
    • Gutierrez, M. G., Munafo, D. B., Beron, W. and Colombo, M. I. (2004) Rab7 is required for the normal progression of the autophagic pathway in mammalian cells. J. Cell Sci. 117, 2687-2697 (Pubitemid 38997252)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2687-2697
    • Gutierrez, M.G.1    Munafo, D.B.2    Beron, W.3    Colombo, M.I.4
  • 15
    • 65349155174 scopus 로고    scopus 로고
    • Early endosomes and endosomal coatomer are required for autophagy
    • Razi, M., Chan, E. Y. and Tooze, S. A. (2009) Early endosomes and endosomal coatomer are required for autophagy. J. Cell Biol. 185, 305-321
    • (2009) J. Cell Biol. , vol.185 , pp. 305-321
    • Razi, M.1    Chan, E.Y.2    Tooze, S.A.3
  • 17
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C. and Klionsky, D. J. (2009) Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43, 67-93
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 18
    • 38549176248 scopus 로고    scopus 로고
    • (the C. elegans Research Community, ed.), doi/10.1895/wormbook.1.9.1
    • Strome, S. (2005) Specification of the germ line, In WormBook (the C. elegans Research Community, ed.), doi/10.1895/wormbook.1.9.1, http://www.wormbook.org
    • (2005) Specification of the Germ Line
    • Strome, S.1
  • 19
    • 0029880495 scopus 로고    scopus 로고
    • Segregation of germ granules in living Caenorhabditis elegans embryos: Cell-type-specific mechanisms for cytoplasmic localisation
    • Hird, S. N., Paulsen, J. E. and Strome, S. (1996) Segregation of germ granules in living Caenorhabditis elegans embryos: cell-type-specific mechanisms for cytoplasmic localisation. Development 122, 1303-1312 (Pubitemid 26124455)
    • (1996) Development , vol.122 , Issue.4 , pp. 1303-1312
    • Hird, S.N.1    Paulsen, J.E.2    Strome, S.3
  • 20
    • 77950483610 scopus 로고    scopus 로고
    • Role of autophagy in Caenorhabditis elegans
    • Kovács, A. L. and Zhang, H. (2010) Role of autophagy in Caenorhabditis elegans. FEBS Lett. 584, 1335-1341
    • (2010) FEBS Lett. , vol.584 , pp. 1335-1341
    • Kovács, A.L.1    Zhang, H.2
  • 21
    • 58249085224 scopus 로고    scopus 로고
    • SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans
    • Zhang, Y. X., Yan, L. B., Zhou, Z., Yang, P. G., Tian, E., Zhang, K., Zhao, Y., Li, Z. P., Song, B., Han, J. H. et al. (2009) SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans. Cell 136, 308-321
    • (2009) Cell , vol.136 , pp. 308-321
    • Zhang, Y.X.1    Yan, L.B.2    Zhou, Z.3    Yang, P.G.4    Tian, E.5    Zhang, K.6    Zhao, Y.7    Li, Z.P.8    Song, B.9    Han, J.H.10
  • 22
    • 0042655132 scopus 로고    scopus 로고
    • Exclusion of germ plasm proteins from somatic lineages by cullin-dependent degradation
    • DOI 10.1038/nature01887
    • DeRenzo, C., Reese, K. J. and Seydoux, G. (2003) Exclusion of germ plasm proteins from somatic lineages by cullin-dependent degradation. Nature 424, 685-689 (Pubitemid 36987994)
    • (2003) Nature , vol.424 , Issue.6949 , pp. 685-689
    • DeRenzo, C.1    Reese, K.J.2    Seydoux, G.3
  • 23
    • 77953713630 scopus 로고    scopus 로고
    • C. elegans screen identifies autophagy genes specific to multicellular organisms
    • Tian, Y., Li, Z. P., Hu, W. Q., Ren, H. Y., Tian, E., Zhao, Y., Lu, Q., Huang, X. X., Yang, P. G., Li, X. et al. (2010) C. elegans screen identifies autophagy genes specific to multicellular organisms. Cell 141, 1042-1055
    • (2010) Cell , vol.141 , pp. 1042-1055
    • Tian, Y.1    Li, Z.P.2    Hu, W.Q.3    Ren, H.Y.4    Tian, E.5    Zhao, Y.6    Lu, Q.7    Huang, X.X.8    Yang, P.G.9    Li, X.10
  • 24
    • 33645926989 scopus 로고    scopus 로고
    • p62/SQSTM1: A missing link between protein aggregates and the autophagy machinery
    • Bjørkøy, G., Lamark, T. and Johansen, T. (2006) p62/SQSTM1: a missing link between protein aggregates and the autophagy machinery. Autophagy 2, 138-139
    • (2006) Autophagy , vol.2 , pp. 138-139
    • Bjørkøy, G.1    Lamark, T.2    Johansen, T.3
  • 25
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • DOI 10.1083/jcb.200507002
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H. and Johansen, T. (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603-614 (Pubitemid 41668720)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 27
    • 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
    • DOI 10.1083/jcb.200711108
    • 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 (Pubitemid 351468465)
    • (2008) Journal of Cell Biology , vol.180 , Issue.6 , 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
  • 30
    • 67650249774 scopus 로고    scopus 로고
    • epg-1 functions in the autophagy pathway and may encode a highly divergent Atg13 homolog in C. elegans
    • Tian, E., Wang, F. X., Han, J. H. and Zhang, H. (2009) epg-1 functions in the autophagy pathway and may encode a highly divergent Atg13 homolog in C. elegans. Autophagy 5, 608-615
    • (2009) Autophagy , vol.5 , pp. 608-615
    • Tian, E.1    Wang, F.X.2    Han, J.H.3    Zhang, H.4
  • 31
    • 84867251783 scopus 로고    scopus 로고
    • The C. elegans AG101 homolog EPG-9 directly interacts with EPG-1/Atg13 and is essential for autophagy
    • Liang, Q. Q., Yang, P. G., Tian, E., Han, J. H. and Zhang, H. (2012) The C. elegans AG101 homolog EPG-9 directly interacts with EPG-1/Atg13 and is essential for autophagy. Autophagy 8, 1426-1433
    • (2012) Autophagy , vol.8 , pp. 1426-1433
    • Liang, Q.Q.1    Yang, P.G.2    Tian, E.3    Han, J.H.4    Zhang, H.5
  • 32
    • 67650216222 scopus 로고    scopus 로고
    • Selective autophagic degradation of maternally-loaded germline P granule components in somatic cells during C. elegans embryogenesis
    • Zhao, Y., Tian, E and Zhang, H. (2009) Selective autophagic degradation of maternally-loaded germline P granule components in somatic cells during C. elegans embryogenesis. Autophagy 5, 717-719
    • (2009) Autophagy , vol.5 , pp. 717-719
    • Zhao, Y.1    Tian, E.2    Zhang, H.3
  • 33
    • 79551539513 scopus 로고    scopus 로고
    • The coiled-coil domain protein EPG-8 plays an essential role in the autophagy pathway in C. elegans
    • Yang, P. G. and Zhang, H. (2011) The coiled-coil domain protein EPG-8 plays an essential role in the autophagy pathway in C. elegans. Autophagy 7, 159-165
    • (2011) Autophagy , vol.7 , pp. 159-165
    • Yang, P.G.1    Zhang, H.2
  • 34
    • 80051474094 scopus 로고    scopus 로고
    • The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes
    • Lu, Q., Yang, P. G., Huang, X. X., Hu, W. Q., Guo, B., Wu, F., Lin, L., Kova'cs, A. L., Yu, L. and Zhang, H. (2011) The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes. Dev. Cell 21, 343-357
    • (2011) Dev. Cell , vol.21 , pp. 343-357
    • Lu, Q.1    Yang, P.G.2    Huang, X.X.3    Hu, W.Q.4    Guo, B.5    Wu, F.6    Lin, L.7    Kova'Cs, A.L.8    Yu, L.9    Zhang, H.10
  • 35
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. (2001) Molecular dissection of autophagy: two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2, 211-216
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 36
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • Kirisako, T., Ichimura, Y., Okada, H., Kabeya, Y., Mizushima, N., Yoshimori, T., Ohsumi, M., Takao, T., Noda, T. and Ohsumi, Y. (2000) The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J. Cell Biol. 151, 263-276
    • (2000) J. Cell Biol. , vol.151 , pp. 263-276
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3    Kabeya, Y.4    Mizushima, N.5    Yoshimori, T.6    Ohsumi, M.7    Takao, T.8    Noda, T.9    Ohsumi, Y.10
  • 38
    • 34447099450 scopus 로고    scopus 로고
    • Atg8, a Ubiquitin-like Protein Required for Autophagosome Formation, Mediates Membrane Tethering and Hemifusion
    • DOI 10.1016/j.cell.2007.05.021, PII S0092867407006587
    • Nakatogawa, H., Ichimura, Y. and Ohsumi, Y. (2007) Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell 130, 165-178 (Pubitemid 47031316)
    • (2007) Cell , vol.130 , Issue.1 , pp. 165-178
    • Nakatogawa, H.1    Ichimura, Y.2    Ohsumi, Y.3
  • 41
    • 0038325675 scopus 로고    scopus 로고
    • Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
    • DOI 10.1242/jcs.00381
    • Mizushima, N., Kuma, A., Kobayashi, Y., Yamamoto, A., Matsubae, M., Takao, T., Nassume, T., Ohsumi, Y. and Yoshimori, T. (2003) Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J. Cell Sci. 116, 1679-1688 (Pubitemid 36582155)
    • (2003) Journal of Cell Science , vol.116 , Issue.9 , pp. 1679-1688
    • Mizushima, N.1    Kuma, A.2    Kobayashi, Y.3    Yamamoto, A.4    Matsubae, M.5    Takao, T.6    Natsume, T.7    Ohsumi, Y.8    Yoshimori, T.9
  • 42
    • 0033565655 scopus 로고    scopus 로고
    • Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway
    • DOI 10.1093/emboj/18.14.3888
    • Mizushima, N., Noda, T. and Ohsumi, Y. (1999) Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. EMBO J. 18, 3888-3896 (Pubitemid 29335842)
    • (1999) EMBO Journal , vol.18 , Issue.14 , pp. 3888-3896
    • Mizushima, N.1    Noda, T.2    Ohsumi, Y.3
  • 43
    • 0037166241 scopus 로고    scopus 로고
    • Formation of the approximately 350-kDa Apg12-Apg5·Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast
    • DOI 10.1074/jbc.M111889200
    • Kuma, A., Mizushima, N., Ishihara, N. and Ohsumi, Y. (2002) Formation of the approximately 350-kDa Apg12-Apg5·Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast. J. Biol. Chem. 277, 18619-18625 (Pubitemid 34952416)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18619-18625
    • Kuma, A.1    Mizushima, N.2    Ishihara, N.3    Ohsumi, Y.4
  • 45
    • 18244394277 scopus 로고    scopus 로고
    • Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy
    • DOI 10.1091/mbc.E04-08-0669
    • Kabeya, Y., Kamada, Y., Baba, M., Takikawa, H., Sasaki, M. and Ohsum, Y. (2005) Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy. Mol. Biol. Cell 16, 2544-2553 (Pubitemid 40632233)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.5 , pp. 2544-2553
    • Kabeya, Y.1    Kamada, Y.2    Baba, M.3    Takikawa, H.4    Sasaki, M.5    Ohsumi, Y.6
  • 46
    • 33947378818 scopus 로고    scopus 로고
    • Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae
    • DOI 10.1016/j.bbrc.2007.02.150, PII S0006291X07004378
    • Kabeya, Y., Kawamata, T., Suzuki, K. and Ohsumi, Y. (2007) Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 356, 405-410 (Pubitemid 46452560)
    • (2007) Biochemical and Biophysical Research Communications , vol.356 , Issue.2 , pp. 405-410
    • Kabeya, Y.1    Kawamata, T.2    Suzuki, K.3    Ohsumi, Y.4
  • 48
    • 43149125546 scopus 로고    scopus 로고
    • Organization of the pre-autophagosomal structure responsible for autophagosome formation
    • Kawamata, T., Kamada, Y., Kabeya, Y., Sekito, T. and Ohsumi, Y. (2008) Organization of the pre-autophagosomal structure responsible for autophagosome formation. Mol. Biol. Cell 19, 2039-2050
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2039-2050
    • Kawamata, T.1    Kamada, Y.2    Kabeya, Y.3    Sekito, T.4    Ohsumi, Y.5
  • 49
    • 39449108917 scopus 로고    scopus 로고
    • The Atg1 kinase complex is involved in the regulation of protein recruitment to initiate sequestering vesicle formation for nonspecific autophagy in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E07-08-0826
    • Cheong, H., Nair, U., Geng, J. and Klionsky, D. J. (2008) The Atg1 kinase complex is involved in the regulation of protein recruitment to initiate sequestering vesicle formation for nonspecific autophagy in Saccharomyces cerevisiae. Mol. Biol. Cell 19, 668-681 (Pubitemid 351272154)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 668-681
    • Cheong, H.1    Nair, U.2    Geng, J.3    Klionsky, D.J.4
  • 50
    • 0030983504 scopus 로고    scopus 로고
    • Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae
    • DOI 10.1016/S0378-1119(97)00084-X, PII S037811199700084X
    • Matsuura, A., Tsukada, M., Wada, Y. and Ohsumi, Y. (1997) Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae. Gene 192, 245-250 (Pubitemid 27268249)
    • (1997) Gene , vol.192 , Issue.2 , pp. 245-250
    • Matsuura, A.1    Tsukada, M.2    Wada, Y.3    Ohsumi, Y.4
  • 51
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
    • DOI 10.1083/jcb.200712064
    • Hara, T., Takamura, A., Kishi, C., Iemura, S., Natsume, T., Guan, J. L. and Mizushima, N. (2008) FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells. J. Cell Biol. 181, 497-510 (Pubitemid 351645039)
    • (2008) Journal of Cell Biology , vol.181 , Issue.3 , pp. 497-510
    • Hara, T.1    Takamura, A.2    Kishi, C.3    Iemura, S.-I.4    Natsume, T.5    Guan, J.-L.6    Mizushima, N.7
  • 53
    • 67549110195 scopus 로고    scopus 로고
    • A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy
    • Mercer, C. A., Kaliappan, A. and Dennis, P. B. (2009) A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy. Autophagy 5, 649-662
    • (2009) Autophagy , vol.5 , pp. 649-662
    • Mercer, C.A.1    Kaliappan, A.2    Dennis, P.B.3
  • 55
    • 66449083078 scopus 로고    scopus 로고
    • ULK1·ATG13·FIP200 complex mediates mTOR signaling and is essential for autophagy
    • Ganley, I. G., Lam, Du, H., Wang, J., Ding, X., Chen, S. and Jiang, X. (2009) ULK1·ATG13·FIP200 complex mediates mTOR signaling and is essential for autophagy. J. Biol. Chem. 284, 12297-12305
    • (2009) J. Biol. Chem. , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    Lam2    Du, H.3    Wang, J.4    Ding, X.5    Chen, S.6    Jiang, X.7
  • 57
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • Mizushima, N. (2010) The role of the Atg1/ULK1 complex in autophagy regulation. Curr. Opin. Cell Biol. 22, 132-139
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 58
    • 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
  • 60
    • 33846514235 scopus 로고    scopus 로고
    • Hierarchy of Atg proteins in pre-autophagosomal structure organization
    • DOI 10.1111/j.1365-2443.2007.01050.x
    • Suzuki, K., Kubota, Y., Sekito, T. and Ohsumi, Y. (2007) Hierarchy of Atg proteins in pre-autophagosomal structure organization. Genes Cells 12, 209-218 (Pubitemid 46152659)
    • (2007) Genes to Cells , vol.12 , Issue.2 , pp. 209-218
    • Suzuki, K.1    Kubota, Y.2    Sekito, T.3    Ohsumi, Y.4
  • 61
    • 44449115788 scopus 로고    scopus 로고
    • Transport of phosphatidylinositol 3-phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae
    • DOI 10.1111/j.1365-2443.2008.01188.x
    • Obara, K., Noda, T., Niimi, K. and Ohsumi, Y. (2008a) Transport of phosphatidylinositol 3-phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae. Genes Cells 13, 537-547 (Pubitemid 351761772)
    • (2008) Genes to Cells , vol.13 , Issue.6 , pp. 537-547
    • Obara, K.1    Noda, T.2    Niimi, K.3    Ohsumi, Y.4
  • 62
    • 33745086418 scopus 로고    scopus 로고
    • Assortment of phosphatidylinositol 3-kinase complexes-Atg14p directs association of complex I to the pre-autophagosomal structure in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E05-09-0841
    • Obara, K., Sekito, T. and Ohsumi, Y. (2006) Assortment of phosphatidylinositol 3-kinase complexes-Atg14p directs association of complex I to the pre-autophagosomal structure in Saccharomyces cerevisiae. Mol. Biol. Cell 17, 1527-1539 (Pubitemid 44011573)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1527-1539
    • Obara, K.1    Sekito, T.2    Ohsumi, Y.3
  • 63
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase y sorting in Saccharomyces cerevisiae
    • Kihara, A., Noda, T., Ishihara, N. and Ohsumi, Y. (2001) Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152, 519-530 (Pubitemid 34280235)
    • (2001) Journal of Cell Biology , vol.153 , Issue.3 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 64
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura, E., Kishi, C., Inoue, K. and Mizushima, N. (2008) Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol. Biol. Cell 19, 5360-5372
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 66
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin1-phosphatidylinositol-3 kinase complex
    • Zhong, Y., Wang, Q. J., Li, X. T., 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 Beclin1-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.T.3    Yan, Y.4    Backer, J.M.5    Chait, B.T.6    Heintz, N.7    Yue, Z.8
  • 67
    • 58049192897 scopus 로고    scopus 로고
    • Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase
    • Sun, Q. M., Fan, W. L., Chen, K. L., Ding, X. J., Chen, S. and Zhong, Q. (2008) Identification of Barkor as a mammalian autophagy-specific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. U.S.A. 105, 19211-19216
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 19211-19216
    • Sun, Q.M.1    Fan, W.L.2    Chen, K.L.3    Ding, X.J.4    Chen, S.5    Zhong, Q.6
  • 68
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang, Z. and Klionsky, D. J. (2010) Mammalian autophagy: core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 22, 124-131
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 69
    • 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
  • 70
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • Yla-Antila, P., Vihinen, H., Jokitalo, E. and Wskelinen, E. L. (2009) 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 5, 1180-1185
    • (2009) Autophagy , vol.5 , pp. 1180-1185
    • Yla-Antila, P.1    Vihinen, H.2    Jokitalo, E.3    Wskelinen, E.L.4
  • 73
    • 53049102656 scopus 로고    scopus 로고
    • The Atg18-Atg2 complex is recruited to autophagic membranes via PtdIns(3)P and exerts an essential function
    • Obara, K., Sekito, T., Niimi, K. and Ohsumi, Y. (2008b) The Atg18-Atg2 complex is recruited to autophagic membranes via PtdIns(3)P and exerts an essential function. J. Biol. Chem. 283, 23972-23980
    • (2008) J. Biol. Chem. , vol.283 , pp. 23972-23980
    • Obara, K.1    Sekito, T.2    Niimi, K.3    Ohsumi, Y.4
  • 74
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation
    • Polson, H. E., de Lartigue, J., Rigden, D. J., Reedijk, M., Urbé, S., Clague, M. J. and Tooze, S. A. (2010) Mammalian Atg18 (WIPI2) localizes to omegasome-anchored 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    Urbé, S.5    Clague, M.J.6    Tooze, S.A.7
  • 75
    • 34447276502 scopus 로고    scopus 로고
    • Human WIPI-1 puncta-formation: A novel assay to assess mammalian autophagy
    • DOI 10.1016/j.febslet.2007.06.040, PII S0014579307006965
    • Proikas-Cezanne, T., Ruckerbauer, S., Stierhof, Y. D., Berg, C. and Nordheim, A. (2007) Human WIPI-1 puncta-formation: a novel assay to assess mammalian autophagy. FEBS Lett. 581, 3396-3404 (Pubitemid 47048184)
    • (2007) FEBS Letters , vol.581 , Issue.18 , pp. 3396-3404
    • Proikas-Cezanne, T.1    Ruckerbauer, S.2    Stierhof, Y.-D.3    Berg, C.4    Nordheim, A.5
  • 76
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C., Sowa, M. E., Gygi, S. P. and Harper, J. W. (2010) Network organization of the human autophagy system. Nature 466, 68-76
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 77
    • 59449097721 scopus 로고    scopus 로고
    • Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy
    • He, C., Baba, M., Cao, Y. and Klionsky, D. J. (2008) Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy. Mol. Biol. Cell 19, 5506-5516
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5506-5516
    • He, C.1    Baba, M.2    Cao, Y.3    Klionsky, D.J.4
  • 78
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • Mari, M., Griffith, J., Rieter, E., Krishnappa, L., Klionsky, D. J. and Reggiori, F. (2010) An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J. Cell Biol. 190, 1005-1022
    • (2010) J. Cell Biol. , vol.190 , pp. 1005-1022
    • Mari, M.1    Griffith, J.2    Rieter, E.3    Krishnappa, L.4    Klionsky, D.J.5    Reggiori, F.6
  • 79
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure
    • DOI 10.1016/S1534-5807(03)00402-7, PII S1534580703004027
    • Reggiori, F., Tucker, K. A., Stromhaug, P. E. and Klionsky, D. J. (2004) The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure. Dev. Cell 6, 79-90 (Pubitemid 38089207)
    • (2004) Developmental Cell , vol.6 , Issue.1 , pp. 79-90
    • Reggiori, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 80
    • 3242888703 scopus 로고    scopus 로고
    • LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
    • DOI 10.1242/jcs.01131
    • Kabeya, Y., Mizushima, N., Yamamoto, A., Oshitani-Okamoto, S., Ohsumi, Y. and Yoshimori, T. (2004) LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation. J. Cell Sci. 117, 2805-2812 (Pubitemid 38997262)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2805-2812
    • Kabeya, Y.1    Mizushima, N.2    Yamamoto, A.3    Oshitani-Okamoto, S.4    Ohsumi, Y.5    Yoshimori, T.6
  • 81
    • 0037515749 scopus 로고    scopus 로고
    • The COOH terminus of GATE-16, an intra-golgi transport modulator, is cleaved by the human cysteine protease HsApg4A
    • DOI 10.1074/jbc.M212108200
    • Scherz-Shouval, R., Sagiv, Y., Shorer, H. and Elazar, Z. (2003) The COOH terminus of GATE-16, an intra-Golgi transport modulator, is cleaved by the human cysteine protease HsApg4A. J. Biol. Chem. 278, 14053-14058 (Pubitemid 36799950)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14053-14058
    • Scherz-Shouval, R.1    Sagiv, Y.2    Shorer, H.3    Elazar, Z.4
  • 82
    • 34547132328 scopus 로고    scopus 로고
    • Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3
    • Mariño, G., Salvador-Montoliu, N., Fueyo, A., Knecht, E., Mizushima, N. and López-Otín, C. (2007) Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3. J. Biol. Chem. 282, 18573-18583
    • (2007) J. Biol. Chem. , vol.282 , pp. 18573-18583
    • Mariño, G.1    Salvador-Montoliu, N.2    Fueyo, A.3    Knecht, E.4    Mizushima, N.5    López-Otín, C.6
  • 83
    • 0347695019 scopus 로고    scopus 로고
    • A Single Protease, Apg4B, Is Specific for the Autophagy-related Ubiquitin-like Proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L
    • DOI 10.1074/jbc.M308762200
    • Hemelaar, J., Lelyveld, V. S., Kessler, B. M. and Ploegh, H. L. (2003) A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L. J. Biol. Chem. 278, 51841-51850 (Pubitemid 38020431)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51841-51850
    • Hemelaar, J.1    Lelyveld, V.S.2    Kessler, B.M.3    Ploegh, H.L.4
  • 84
    • 4344604111 scopus 로고    scopus 로고
    • A receptor-associated protein-phospholipid conjugates
    • DOI 10.1074/jbc.M401461200
    • Tanida, I., Sou, Y., Ezaki, J., Minematsu-Ikeguchi, N., Ueno, T. and Kominami, E. (2004) HsAtg4B/HsApg4B/Autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates. J. Biol. Chem. 279, 36268-36276 (Pubitemid 39128963)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36268-36276
    • Tanida, I.1    Sou, Y.-S.2    Ezaki, J.3    Minematsu-Ikeguchi, N.4    Ueno, T.5    Kominami, E.6
  • 85
    • 79953190772 scopus 로고    scopus 로고
    • Kinetics comparisons of mammalian Atg4 homologues indicate selective preferences toward diverse Atg8 substrates
    • Li, M., Hou, Y., Wang, J., Chen, X., Shao, Z. M. and Yin, X. M. (2011) Kinetics comparisons of mammalian Atg4 homologues indicate selective preferences toward diverse Atg8 substrates. J. Biol. Chem. 286, 7327-7338
    • (2011) J. Biol. Chem. , vol.286 , pp. 7327-7338
    • Li, M.1    Hou, Y.2    Wang, J.3    Chen, X.4    Shao, Z.M.5    Yin, X.M.6
  • 86
    • 84865518164 scopus 로고    scopus 로고
    • Differential function of the two Atg4 homologues in the aggrephagy pathway in Caenorhabditis elegans
    • Wu, F., Li, Y. P., Wang, F. X., Noda, N. N. and Zhang, H. (2012) Differential function of the two Atg4 homologues in the aggrephagy pathway in Caenorhabditis elegans. J. Biol. Chem. 287, 29457-29467
    • (2012) J. Biol. Chem. , vol.287 , pp. 29457-29467
    • Wu, F.1    Li, Y.P.2    Wang, F.X.3    Noda, N.N.4    Zhang, H.5
  • 87
    • 84857256919 scopus 로고    scopus 로고
    • Atg4 recycles inappropriately lapidated Atg8 to promote autophagosome biogenesis
    • Nakatogawa, H., Ishii, J., Asai, E. and Ohsumi, Y. (2012) Atg4 recycles inappropriately lapidated Atg8 to promote autophagosome biogenesis. Autophagy 8, 1-10
    • (2012) Autophagy , vol.8 , pp. 1-10
    • Nakatogawa, H.1    Ishii, J.2    Asai, E.3    Ohsumi, Y.4
  • 89
  • 90
    • 0029917987 scopus 로고    scopus 로고
    • Identification and cloning of EI24, a gene induced by p53 in etoposide-treated cells
    • Lehar, S. M., Nacht, M., Jacks, T., Vater, C. A., Chittenden, T. and Guild, B. C. (1996) Identification and cloning of EI24, a gene induced by p53 in etoposide-treated cells. Oncogene 12, 1181-1187 (Pubitemid 26127248)
    • (1996) Oncogene , vol.12 , Issue.6 , pp. 1181-1187
    • Lehar, S.M.1    Nacht, M.2    Jacks, T.3    Vater, C.A.4    Chittenden, T.5    Guild, B.C.6
  • 91
    • 84871282033 scopus 로고    scopus 로고
    • The p53-induced gene Ei24 is an essential component of the basal autophagy pathway
    • Zhao, G. Y., Zhao, H. Y., Miao, L., Wang, L., Sun, F. and Zhang, H. (2012) The p53-induced gene Ei24 is an essential component of the basal autophagy pathway. J. Biol. Chem. 287, 42053-42063
    • (2012) J. Biol. Chem. , vol.287 , pp. 42053-42063
    • Zhao, G.Y.1    Zhao, H.Y.2    Miao, L.3    Wang, L.4    Sun, F.5    Zhang, H.6
  • 97
    • 0035031192 scopus 로고    scopus 로고
    • Regulation of endocytosis by CUP-5, the Caenorhabditis elegans mucolipin-1 homolog
    • DOI 10.1038/88281
    • Fares, H. and Greenwald, I. (2001) Regulation of endocytosis by CUP-5, the Caenorhabditis elegans mucolipin-1 homolog. Nat. Genet. 28, 64-68 (Pubitemid 32405819)
    • (2001) Nature Genetics , vol.28 , Issue.1 , pp. 64-68
    • Fares, H.1    Greenwald, I.2
  • 99
    • 80655134746 scopus 로고    scopus 로고
    • CUP-5, the C. elegans ortholog of the mammalian lysosomal channel protein MLN1/TRPML1, is required for proteolytic degradation in autolysosomes
    • Sun, T., Wang, X. W., Lu, Q., Ren, H. Y. and Zhang, H. (2011) CUP-5, the C. elegans ortholog of the mammalian lysosomal channel protein MLN1/TRPML1, is required for proteolytic degradation in autolysosomes. Autophagy 7, 1308-1315
    • (2011) Autophagy , vol.7 , pp. 1308-1315
    • Sun, T.1    Wang, X.W.2    Lu, Q.3    Ren, H.Y.4    Zhang, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.