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Volumn 1792, Issue 1, 2009, Pages 3-13

Autophagy: Principles and significance in health and disease

Author keywords

ATG genes; Autophagosome; Autophagy; Lysosome; Vacuole; Yeast

Indexed keywords

BECLIN 1; CHAPERONE; METHANOL; NITROGEN; PHOSPHATIDYLINOSITOL 3 KINASE;

EID: 57849136841     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2008.10.016     Document Type: Review
Times cited : (285)

References (112)
  • 1
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada M., and Oshumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS lett. 333 (1993) 169-174
    • (1993) FEBS lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Oshumi, Y.2
  • 2
    • 24744441497 scopus 로고    scopus 로고
    • Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation
    • Onodera J., and Oshumi Y. Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation. J. Biol. Chem. 280 (2005) 31582-31586
    • (2005) J. Biol. Chem. , vol.280 , pp. 31582-31586
    • Onodera, J.1    Oshumi, Y.2
  • 3
    • 33845407202 scopus 로고    scopus 로고
    • Atg22 recycles amino acids to link the degradative and recycling functions of autophagy
    • Yang Z., Huang J., Geng J., Nair U., and Klionsky D.J. Atg22 recycles amino acids to link the degradative and recycling functions of autophagy. Mol. Biol. Cell 17 (2006) 5094-5104
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5094-5104
    • Yang, Z.1    Huang, J.2    Geng, J.3    Nair, U.4    Klionsky, D.J.5
  • 4
    • 33749055522 scopus 로고    scopus 로고
    • Autophagy: a cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically
    • Bergamini E. Autophagy: a cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically. Mol. Aspects Med. 27 (2006) 403-410
    • (2006) Mol. Aspects Med. , vol.27 , pp. 403-410
    • Bergamini, E.1
  • 5
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • Levine B., and Klionsky D.J. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 6 (2004) 463-477
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 6
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., Levine B., Cuervo A.M., and Klionsky D.J. Autophagy fights disease through cellular self-digestion. Nature 451 (2008) 1069-1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 7
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: protection against neurodegeneration and ageing
    • Tatsuta T., and Langer T. Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J. 27 (2008) 306-314
    • (2008) EMBO J. , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 8
    • 33745879143 scopus 로고    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. Exp. Biol. Med. (Maywood) 231 (2006) 1197-1211
    • (2006) Exp. Biol. Med. (Maywood) , vol.231 , pp. 1197-1211
    • Ciechanover, A.1
  • 9
    • 33748413303 scopus 로고    scopus 로고
    • Intracellular quality control by autophagy: how does autophagy prevent neurodegeneration?
    • Mizushima N., and Hara T. Intracellular quality control by autophagy: how does autophagy prevent neurodegeneration?. Autophagy 2 (2006) 302-304
    • (2006) Autophagy , vol.2 , pp. 302-304
    • Mizushima, N.1    Hara, T.2
  • 10
  • 11
    • 2942624168 scopus 로고    scopus 로고
    • Microautophagy and macropexophagy may occur simultaneously in Hansenula polymorpha
    • Monastryska I., Sjollema K., van der Klei I.J., Kiel J.A., and Veenhuis M. Microautophagy and macropexophagy may occur simultaneously in Hansenula polymorpha. FEBS Lett. 568 (2004) 135-138
    • (2004) FEBS Lett. , vol.568 , pp. 135-138
    • Monastryska, I.1    Sjollema, K.2    van der Klei, I.J.3    Kiel, J.A.4    Veenhuis, M.5
  • 12
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice J.F. Chaperone-mediated autophagy. Autophagy 3 (2007) 295-299
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 13
    • 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 (1990) 305-309
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 14
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • Chiang H.L., and Dice J.F. Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J. Biol. Chem. 263 (1988) 6797-6805
    • (1988) J. Biol. Chem. , vol.263 , pp. 6797-6805
    • Chiang, H.L.1    Dice, J.F.2
  • 16
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: unanswered questions
    • Klionsky D.J. The molecular machinery of autophagy: unanswered questions. J. Cell Sci. 118 (2005) 7-18
    • (2005) J. Cell Sci. , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 17
    • 33947383050 scopus 로고    scopus 로고
    • ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes
    • Meijer W.H., van der Klei I.J., Veenhuis M., and Kiel J.A. ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes. Autophagy 3 (2007) 106-116
    • (2007) Autophagy , vol.3 , pp. 106-116
    • Meijer, W.H.1    van der Klei, I.J.2    Veenhuis, M.3    Kiel, J.A.4
  • 18
    • 41749114288 scopus 로고    scopus 로고
    • Autophagy: basic principles and relevance to disease
    • Kundu M., and Thompson C.B. Autophagy: basic principles and relevance to disease. Annu. Rev. Pathol. 3 (2008) 427-455
    • (2008) Annu. Rev. Pathol. , vol.3 , pp. 427-455
    • Kundu, M.1    Thompson, C.B.2
  • 19
    • 38749136302 scopus 로고    scopus 로고
    • Regulation of macroautophagy by mTOR and Beclin 1 complexes
    • Pattingre S., Espert L., Biard-Piechaczyk M., and Codogno P. Regulation of macroautophagy by mTOR and Beclin 1 complexes. Biochimie 90 (2008) 313-323
    • (2008) Biochimie , vol.90 , pp. 313-323
    • Pattingre, S.1    Espert, L.2    Biard-Piechaczyk, M.3    Codogno, P.4
  • 20
    • 0030919092 scopus 로고    scopus 로고
    • Analyses of APG13 gene involved in autophagy in yeast, Saccharomyces cerevisiae
    • Funakoshi T., Matsuura A., Noda T., and Ohsumi Y. Analyses of APG13 gene involved in autophagy in yeast, Saccharomyces cerevisiae. Gene 192 (1997) 207-213
    • (1997) Gene , vol.192 , pp. 207-213
    • Funakoshi, T.1    Matsuura, A.2    Noda, T.3    Ohsumi, Y.4
  • 23
    • 0030983504 scopus 로고    scopus 로고
    • Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae
    • Matsuura A., Tsukada M., Wada Y., and Ohsumi Y. Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae. Gene 192 (1997) 245-250
    • (1997) Gene , vol.192 , pp. 245-250
    • Matsuura, A.1    Tsukada, M.2    Wada, Y.3    Ohsumi, Y.4
  • 24
    • 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. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152 (2001) 519-530
    • (2001) J. Cell Biol. , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 25
    • 0032575551 scopus 로고    scopus 로고
    • Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae
    • Kametaka S., Okano T., Ohsumi M., and Ohsumi Y. Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 22284-22291
    • (1998) J. Biol. Chem. , vol.273 , pp. 22284-22291
    • Kametaka, S.1    Okano, T.2    Ohsumi, M.3    Ohsumi, Y.4
  • 26
    • 0035503594 scopus 로고    scopus 로고
    • The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
    • Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., and Ohsumi Y. The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO J. 20 (2001) 5971-5981
    • (2001) EMBO J. , vol.20 , pp. 5971-5981
    • Suzuki, K.1    Kirisako, T.2    Kamada, Y.3    Mizushima, N.4    Noda, T.5    Ohsumi, Y.6
  • 27
    • 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. Organization of the pre-autophagosomal structure responsible for autophagosome formation. Mol. Biol. Cell (2008) 2039-2050
    • (2008) Mol. Biol. Cell , pp. 2039-2050
    • Kawamata, T.1    Kamada, Y.2    Kabeya, Y.3    Sekito, T.4    Ohsumi, Y.5
  • 28
    • 22044442015 scopus 로고    scopus 로고
    • Autophagosomes: biogenesis from scratch?
    • Reggiori F., and Klionsky D.J. Autophagosomes: biogenesis from scratch?. Curr. Opin. Cell Biol. 17 (2005) 415-422
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 415-422
    • Reggiori, F.1    Klionsky, D.J.2
  • 29
    • 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. 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 (2000) 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
  • 30
    • 0032126632 scopus 로고    scopus 로고
    • Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole
    • Lang T., Schaeffeler E., Bernreuther D., Bredschneider M., Wolf D.H., and Thumm M. Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole. EMBO J. 17 (1998) 3597-3607
    • (1998) EMBO J. , vol.17 , pp. 3597-3607
    • Lang, T.1    Schaeffeler, E.2    Bernreuther, D.3    Bredschneider, M.4    Wolf, D.H.5    Thumm, M.6
  • 31
    • 0141964578 scopus 로고    scopus 로고
    • Modification of a ubiquitin-like protein Paz2 conducted micropexophagy through formation of a novel membrane structure
    • Mukaiyama H., Baba M., Osumi M., Aoyagi S., Kato N., Ohsumi Y., and Sakai Y. Modification of a ubiquitin-like protein Paz2 conducted micropexophagy through formation of a novel membrane structure. Mol. Biol. Cell 15 (2004) 58-70
    • (2004) Mol. Biol. Cell , vol.15 , pp. 58-70
    • Mukaiyama, H.1    Baba, M.2    Osumi, M.3    Aoyagi, S.4    Kato, N.5    Ohsumi, Y.6    Sakai, Y.7
  • 32
    • 0036163982 scopus 로고    scopus 로고
    • Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of peroxisomes during macropexophagy
    • Mukaiyama H., Oku M., Baba M., Samizo T., Hammond A.T., Glick B.S., Kato N., and Sakai Y. Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of peroxisomes during macropexophagy. Genes Cells 7 (2002) 75-90
    • (2002) Genes Cells , vol.7 , pp. 75-90
    • Mukaiyama, H.1    Oku, M.2    Baba, M.3    Samizo, T.4    Hammond, A.T.5    Glick, B.S.6    Kato, N.7    Sakai, Y.8
  • 33
    • 0032896760 scopus 로고    scopus 로고
    • Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways
    • Kim J., Dalton V.M., Eggerton K.P., Scott S.V., and Klionsky D.J. Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways. Mol. Biol. Cell 10 (1999) 1337-1351
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1337-1351
    • Kim, J.1    Dalton, V.M.2    Eggerton, K.P.3    Scott, S.V.4    Klionsky, D.J.5
  • 34
    • 0032895859 scopus 로고    scopus 로고
    • Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein
    • Yuan W., Stromhaug P.E., and Jr Dunn W.A. Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein. Mol. Biol. Cell 10 (1999) 1353-1366
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1353-1366
    • Yuan, W.1    Stromhaug, P.E.2    Jr Dunn, W.A.3
  • 38
    • 0033565655 scopus 로고    scopus 로고
    • Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway
    • Mizushima N., Noda T., and Ohsumi Y. Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. EMBO J. 18 (1999) 3888-3896
    • (1999) EMBO J. , vol.18 , pp. 3888-3896
    • Mizushima, N.1    Noda, T.2    Ohsumi, Y.3
  • 39
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure
    • Reggiori F., Tucker K.A., Stromhaug P.E., and Klionsky D.J. The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure. Dev. Cell 6 (2004) 79-90
    • (2004) Dev. Cell , vol.6 , pp. 79-90
    • Reggiori, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 41
    • 34248572712 scopus 로고    scopus 로고
    • A cytoplasm to vacuole targeting pathway in P. pastoris
    • Farré J.C., Vidal J., and Subramani S. A cytoplasm to vacuole targeting pathway in P. pastoris. Autophagy 3 (2007) 230-234
    • (2007) Autophagy , vol.3 , pp. 230-234
    • Farré, J.C.1    Vidal, J.2    Subramani, S.3
  • 42
    • 0034964443 scopus 로고    scopus 로고
    • Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway
    • Scott S.V., Guan J., Hutchins M.U., Kim J., and Klionsky D.J. Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway. Mol. Cell 7 (2001) 1131-1141
    • (2001) Mol. Cell , vol.7 , pp. 1131-1141
    • Scott, S.V.1    Guan, J.2    Hutchins, M.U.3    Kim, J.4    Klionsky, D.J.5
  • 43
    • 0036901104 scopus 로고    scopus 로고
    • Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway
    • Shintani T., Huang W.P., Stromhaug P.E., and Klionsky D.J. Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway. Dev. Cell 3 (2002) 825-837
    • (2002) Dev. Cell , vol.3 , pp. 825-837
    • Shintani, T.1    Huang, W.P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 44
    • 0036702197 scopus 로고    scopus 로고
    • Molecular machinery required for autophagy and the cytoplasm to vacuole targeting (Cvt) pathway in S. cerevisiae
    • Khalfan W.A., and Klionsky D.J. Molecular machinery required for autophagy and the cytoplasm to vacuole targeting (Cvt) pathway in S. cerevisiae. Curr. Opin. Cell Biol. 14 (2002) 468-475
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 468-475
    • Khalfan, W.A.1    Klionsky, D.J.2
  • 45
    • 0018090257 scopus 로고
    • Degradation of microbodies in relation to activities of alcohol oxidase and catalase in Candida boidinii
    • Bormann C., and Sahm H. Degradation of microbodies in relation to activities of alcohol oxidase and catalase in Candida boidinii. Arch. Microbiol. 117 (1978) 67-72
    • (1978) Arch. Microbiol. , vol.117 , pp. 67-72
    • Bormann, C.1    Sahm, H.2
  • 46
    • 0017820576 scopus 로고
    • Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymorpha and its relation to environmental conditions
    • Veenhuis M., van Dijken J.P., Pilon S.A., and Harder W. Development of crystalline peroxisomes in methanol-grown cells of the yeast Hansenula polymorpha and its relation to environmental conditions. Arch. Microbiol. 117 (1978) 153-163
    • (1978) Arch. Microbiol. , vol.117 , pp. 153-163
    • Veenhuis, M.1    van Dijken, J.P.2    Pilon, S.A.3    Harder, W.4
  • 47
    • 0020772844 scopus 로고
    • Degradation and turnover of peroxisomes in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes
    • Veenhuis M., Douma A., Harder W., and Osumi M. Degradation and turnover of peroxisomes in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes. Arch Microbiol. 134 (1983) 193-203
    • (1983) Arch Microbiol. , vol.134 , pp. 193-203
    • Veenhuis, M.1    Douma, A.2    Harder, W.3    Osumi, M.4
  • 48
    • 0028855325 scopus 로고
    • Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris
    • Tuttle D.L., and Dunn Jr. W.A. Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris. J. Cell Sci. 108 (1995) 25-35
    • (1995) J. Cell Sci. , vol.108 , pp. 25-35
    • Tuttle, D.L.1    Dunn Jr., W.A.2
  • 49
    • 0027207680 scopus 로고
    • Selective autophagy of peroxisomes in methylotrophic yeasts
    • Tuttle D.L., Lewin A.S., and Jr Dunn W.A. Selective autophagy of peroxisomes in methylotrophic yeasts. Eur. J. Cell Biol. 60 (1993) 283-290
    • (1993) Eur. J. Cell Biol. , vol.60 , pp. 283-290
    • Tuttle, D.L.1    Lewin, A.S.2    Jr Dunn, W.A.3
  • 51
    • 0037044768 scopus 로고    scopus 로고
    • Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha
    • Bellu A.R., Salomons F.A., Kiel J.A., Veenhuis M., and Van der Klei I.J. Removal of Pex3p is an important initial stage in selective peroxisome degradation in Hansenula polymorpha. J. Biol. Chem. 277 (2002) 42875-42880
    • (2002) J. Biol. Chem. , vol.277 , pp. 42875-42880
    • Bellu, A.R.1    Salomons, F.A.2    Kiel, J.A.3    Veenhuis, M.4    Van der Klei, I.J.5
  • 52
    • 33745820846 scopus 로고    scopus 로고
    • Pex14p is not required for N-starvation induced microautophagy and in catalytic amounts for macropexophagy in Hansenula polymorpha
    • de Vries B., Todde V., Stevens P., Salomons F., van der Klei I.J., and Veenhuis M. Pex14p is not required for N-starvation induced microautophagy and in catalytic amounts for macropexophagy in Hansenula polymorpha. Autophagy 23 (2006) 183-188
    • (2006) Autophagy , vol.23 , pp. 183-188
    • de Vries, B.1    Todde, V.2    Stevens, P.3    Salomons, F.4    van der Klei, I.J.5    Veenhuis, M.6
  • 53
    • 38049062944 scopus 로고    scopus 로고
    • Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy
    • van Zutphen T., Veenhuis M., and van der Klei I.J. Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy. Autophagy 4 (2008) 63-66
    • (2008) Autophagy , vol.4 , pp. 63-66
    • van Zutphen, T.1    Veenhuis, M.2    van der Klei, I.J.3
  • 54
    • 41949118972 scopus 로고    scopus 로고
    • Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation
    • Nagotu S., Saraya R., Otzen M., Veenhuis M., and van der Klei I.J. Peroxisome proliferation in Hansenula polymorpha requires Dnm1p which mediates fission but not de novo formation. Biochim. Biophys. Acta 1783 (2008) 760-769
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 760-769
    • Nagotu, S.1    Saraya, R.2    Otzen, M.3    Veenhuis, M.4    van der Klei, I.J.5
  • 55
    • 34547595860 scopus 로고    scopus 로고
    • Yeast peroxisomes multiply by growth and division
    • Motley A.M., and Hettema E.H. Yeast peroxisomes multiply by growth and division. J. Cell Biol. 178 (2007) 399-410
    • (2007) J. Cell Biol. , vol.178 , pp. 399-410
    • Motley, A.M.1    Hettema, E.H.2
  • 56
    • 2442581274 scopus 로고    scopus 로고
    • Transcriptional down-regulation of peroxisome numbers affects selective peroxisome degradation in Hansenula polymorpha
    • Leao-Helder A.N., Krikken A.M., van der Klei I.J., Kiel J.A., and Veenhuis M. Transcriptional down-regulation of peroxisome numbers affects selective peroxisome degradation in Hansenula polymorpha. J. Biol. Chem. 278 (2003) 40749-40756
    • (2003) J. Biol. Chem. , vol.278 , pp. 40749-40756
    • Leao-Helder, A.N.1    Krikken, A.M.2    van der Klei, I.J.3    Kiel, J.A.4    Veenhuis, M.5
  • 58
    • 34248581851 scopus 로고    scopus 로고
    • ER-phagy: selective autophagy of the endoplasmic reticulum
    • Bernales S., Schuck S., and Walter P. ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy 3 (2007) 285-287
    • (2007) Autophagy , vol.3 , pp. 285-287
    • Bernales, S.1    Schuck, S.2    Walter, P.3
  • 59
    • 34548077177 scopus 로고    scopus 로고
    • Autophagy and vacuole homeostasis: a case for self-degradation?
    • Mijaljica D., Prescott M., Klionsky D.J., and Devenish R.J. Autophagy and vacuole homeostasis: a case for self-degradation?. Autophagy 3 (2007) 417-421
    • (2007) Autophagy , vol.3 , pp. 417-421
    • Mijaljica, D.1    Prescott, M.2    Klionsky, D.J.3    Devenish, R.J.4
  • 60
    • 21244448694 scopus 로고    scopus 로고
    • The TOR and EGO protein complexes orchestrate microautophagy in yeast
    • Dubouloz F., Deloche O., Wanke V., Cameroni E., and De Virgilio C. The TOR and EGO protein complexes orchestrate microautophagy in yeast. Mol. Cell 19 (2005) 15-26
    • (2005) Mol. Cell , vol.19 , pp. 15-26
    • Dubouloz, F.1    Deloche, O.2    Wanke, V.3    Cameroni, E.4    De Virgilio, C.5
  • 61
    • 84934440405 scopus 로고    scopus 로고
    • Microautophagy in the yeast Saccharomyces cerevisiae
    • Uttenweiler A., and Mayer A. Microautophagy in the yeast Saccharomyces cerevisiae. Methods Mol. Biol. 445 (2008) 245-259
    • (2008) Methods Mol. Biol. , vol.445 , pp. 245-259
    • Uttenweiler, A.1    Mayer, A.2
  • 62
    • 33846116102 scopus 로고    scopus 로고
    • The vacuolar transporter chaperone (VTC) complex is required for microautophagy
    • Uttenweiler A., Schwarz H., Neumann H., and Mayer A. The vacuolar transporter chaperone (VTC) complex is required for microautophagy. Mol. Biol. Cell 18 (2007) 166-175
    • (2007) Mol. Biol. Cell , vol.18 , pp. 166-175
    • Uttenweiler, A.1    Schwarz, H.2    Neumann, H.3    Mayer, A.4
  • 63
    • 0034735536 scopus 로고    scopus 로고
    • Autophagic tubes: vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding
    • Müller O., Sattler T., Flötenmeyer M., Schwarz H., Plattner H., and Mayer A. Autophagic tubes: vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding. J. Cell Biol. 151 (2000) 519-528
    • (2000) J. Cell Biol. , vol.151 , pp. 519-528
    • Müller, O.1    Sattler, T.2    Flötenmeyer, M.3    Schwarz, H.4    Plattner, H.5    Mayer, A.6
  • 65
    • 0030883562 scopus 로고    scopus 로고
    • Glucose-induced microautophagy in Pichia pastoris requires the alpha-subunit of phosphofructokinase
    • Yuan W., Tuttle D.L., Shi Y.J., Ralph G.S., and Jr Dunn W.A. Glucose-induced microautophagy in Pichia pastoris requires the alpha-subunit of phosphofructokinase. J. Cell. Sci. 110 (1997) 1935-1945
    • (1997) J. Cell. Sci. , vol.110 , pp. 1935-1945
    • Yuan, W.1    Tuttle, D.L.2    Shi, Y.J.3    Ralph, G.S.4    Jr Dunn, W.A.5
  • 66
  • 67
    • 33748434220 scopus 로고    scopus 로고
    • Role of Vac8 in formation of the vacuolar sequestering membrane during macropexophagy
    • Oku M., Nishimura T., Hattori T., Ano Y., Yamashita S., and Sakai Y. Role of Vac8 in formation of the vacuolar sequestering membrane during macropexophagy. Autophagy 2 (2006) 272-279
    • (2006) Autophagy , vol.2 , pp. 272-279
    • Oku, M.1    Nishimura, T.2    Hattori, T.3    Ano, Y.4    Yamashita, S.5    Sakai, Y.6
  • 68
    • 42049094041 scopus 로고    scopus 로고
    • PpAtg30 tags peroxisomes for turnover by selective autophagy
    • Farré J.C., Manjithaya R., Mathewson R.D., and Subramani S. PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev. Cell 14 (2008) 365-376
    • (2008) Dev. Cell , vol.14 , pp. 365-376
    • Farré, J.C.1    Manjithaya, R.2    Mathewson, R.D.3    Subramani, S.4
  • 70
    • 33947375637 scopus 로고    scopus 로고
    • Nucleus-vacuole junctions and piecemeal microautophagy of the nucleus in S. cerevisiae
    • Kvam E., and Goldfarb D.S. Nucleus-vacuole junctions and piecemeal microautophagy of the nucleus in S. cerevisiae. Autophagy 3 (2007) 85-92
    • (2007) Autophagy , vol.3 , pp. 85-92
    • Kvam, E.1    Goldfarb, D.S.2
  • 71
    • 24344449583 scopus 로고    scopus 로고
    • Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles
    • Kvam E., Gable K., Dunn T.M., and Goldfarb D.S. Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol. Biol. Cell 16 (2005) 3987-3998
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3987-3998
    • Kvam, E.1    Gable, K.2    Dunn, T.M.3    Goldfarb, D.S.4
  • 73
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissová I., Deffieu M., Manon S., and Camougrand N. Uth1p is involved in the autophagic degradation of mitochondria. J. Biol. Chem. 279 (2004) 39068-39074
    • (2004) J. Biol. Chem. , vol.279 , pp. 39068-39074
    • Kissová, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 74
    • 34247172582 scopus 로고    scopus 로고
    • Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival
    • Tal R., Winter G., Ecker N., Klionsky D.J., and Abeliovich H. Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival. J. Biol. Chem. 282 (2007) 5617-5624
    • (2007) J. Biol. Chem. , vol.282 , pp. 5617-5624
    • Tal, R.1    Winter, G.2    Ecker, N.3    Klionsky, D.J.4    Abeliovich, H.5
  • 75
    • 34250898919 scopus 로고    scopus 로고
    • Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy
    • Nowikovsky K., Reipert S., Devenish R.J., and Schweyen R.J. Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy. Cell Death Differ. 14 (2007) 1647-1656
    • (2007) Cell Death Differ. , vol.14 , pp. 1647-1656
    • Nowikovsky, K.1    Reipert, S.2    Devenish, R.J.3    Schweyen, R.J.4
  • 78
    • 35348886043 scopus 로고    scopus 로고
    • Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein
    • Cao Y., and Klionsky K.J. Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein. Cell Res. 17 (2007) 839-849
    • (2007) Cell Res. , vol.17 , pp. 839-849
    • Cao, Y.1    Klionsky, K.J.2
  • 79
    • 51449085299 scopus 로고    scopus 로고
    • The role of autophagy in mammalian development: cell makeover rather than cell death
    • Cecconi F., and Levine B. The role of autophagy in mammalian development: cell makeover rather than cell death. Dev. Cell 15 (2008) 344-357
    • (2008) Dev. Cell , vol.15 , pp. 344-357
    • Cecconi, F.1    Levine, B.2
  • 80
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B., and Kroemer G. Autophagy in the pathogenesis of disease. Cell 32 (2008) 27-42
    • (2008) Cell , vol.32 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 83
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 (2004) S10-17
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 85
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., Stenmark H., and Johansen T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171 (2005) 603-614
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 86
    • 33645926989 scopus 로고    scopus 로고
    • p62/SQSTM1: a missing link between protein aggregates and the autophagy machinery
    • Bjørkøy G., Lamark T., and Johansen T. p62/SQSTM1: a missing link between protein aggregates and the autophagy machinery. Autophagy 2 (2006) 138-139
    • (2006) Autophagy , vol.2 , pp. 138-139
    • Bjørkøy, G.1    Lamark, T.2    Johansen, T.3
  • 90
    • 33750322790 scopus 로고    scopus 로고
    • Autophagy in innate immunity against intracellular bacteria
    • Amano A., Nakagawa I., and Yoshimori T. Autophagy in innate immunity against intracellular bacteria. J. Biochem. 140 (2006) 161-166
    • (2006) J. Biochem. , vol.140 , pp. 161-166
    • Amano, A.1    Nakagawa, I.2    Yoshimori, T.3
  • 93
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Liu Y., Schiff M., Czymmek K., Talloczy Z., Levine B., and Dinesh-Kumar S.P. Autophagy regulates programmed cell death during the plant innate immune response. Cell 121 (2005) 567-577
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1    Schiff, M.2    Czymmek, K.3    Talloczy, Z.4    Levine, B.5    Dinesh-Kumar, S.P.6
  • 95
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S., and Krijnse-Locker J. Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6 (2008) 363-374
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 97
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice E., Jerome W.G., Yoshimori T., Mizushima N., and Denison M.R. Coronavirus replication complex formation utilizes components of cellular autophagy. J. Biol. Chem. 279 (2004) 10136-10141
    • (2004) J. Biol. Chem. , vol.279 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 99
    • 39149117352 scopus 로고    scopus 로고
    • Autophagy and antiviral immunity
    • Lee H.K., and Iwasaki A. Autophagy and antiviral immunity. Curr. Opin. Immunol. 20 (2008) 23-29
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 23-29
    • Lee, H.K.1    Iwasaki, A.2
  • 103
    • 34548451974 scopus 로고    scopus 로고
    • Reactive oxygen species in mitochondria-mediated cell death
    • Orrenius S. Reactive oxygen species in mitochondria-mediated cell death. Drug Metab. Rev. 39 (2007) 443-455
    • (2007) Drug Metab. Rev. , vol.39 , pp. 443-455
    • Orrenius, S.1
  • 104
    • 34447132925 scopus 로고    scopus 로고
    • Sodium selenite induces superoxide-mediated mitochondrial damage and subsequent autophagic cell death in malignant glioma cells
    • Kim E.H., Sohn S., Kwon H.J., Kim S.U., Kim M.J., Lee S.J., and Choi K.S. Sodium selenite induces superoxide-mediated mitochondrial damage and subsequent autophagic cell death in malignant glioma cells. Cancer Res. 67 (2007) 6314-6324
    • (2007) Cancer Res. , vol.67 , pp. 6314-6324
    • Kim, E.H.1    Sohn, S.2    Kwon, H.J.3    Kim, S.U.4    Kim, M.J.5    Lee, S.J.6    Choi, K.S.7
  • 105
    • 33845292901 scopus 로고    scopus 로고
    • Peroxisomes and oxidative stress
    • Schrader M., and Fahimi H.D. Peroxisomes and oxidative stress. Biochim. Biophys. Acta 1763 (2006) 1755-1766
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1755-1766
    • Schrader, M.1    Fahimi, H.D.2
  • 106
    • 33947374361 scopus 로고    scopus 로고
    • A peroxisomal lon protease and peroxisome degradation by autophagy play key roles in vitality of Hansenula polymorpha cells
    • Aksam E.B., Koek A., Kiel J.A., Jourdan S., Veenhuis M., and van der Klei I.J. A peroxisomal lon protease and peroxisome degradation by autophagy play key roles in vitality of Hansenula polymorpha cells. Autophagy 3 (2007) 96-105
    • (2007) Autophagy , vol.3 , pp. 96-105
    • Aksam, E.B.1    Koek, A.2    Kiel, J.A.3    Jourdan, S.4    Veenhuis, M.5    van der Klei, I.J.6
  • 107
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft C., Deplazes A., Sohrmann M., and Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell Biol. 10 (2008) 602-610
    • (2008) Nat. Cell Biol. , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 108
    • 33744755382 scopus 로고    scopus 로고
    • Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein
    • Ohsaki Y., Cheng J., Fujita A., Tokumoto T., and Fujimoto T. Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein. Mol. Biol. Cell 17 (2006) 2674-2683
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2674-2683
    • Ohsaki, Y.1    Cheng, J.2    Fujita, A.3    Tokumoto, T.4    Fujimoto, T.5
  • 109
    • 0034898851 scopus 로고    scopus 로고
    • Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-Activated protein kinase, and the cyclin-dependent kinase Pho85p
    • Wang Z., Wilson W.A., Fujino M.A., and Roach P.J. Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-Activated protein kinase, and the cyclin-dependent kinase Pho85p. Mol. Cell Biol. 21 (2001) 5742-5752
    • (2001) Mol. Cell Biol. , vol.21 , pp. 5742-5752
    • Wang, Z.1    Wilson, W.A.2    Fujino, M.A.3    Roach, P.J.4
  • 110
    • 0034809331 scopus 로고    scopus 로고
    • Aut5/Cvt17p, a putative lipase essential for disintegration of autophagic bodies inside the vacuole
    • Epple U.D., Suriapranata I., Eskelinen E.L., and Thumm M. Aut5/Cvt17p, a putative lipase essential for disintegration of autophagic bodies inside the vacuole. J. Bacteriol. 183 (2001) 5942-5955
    • (2001) J. Bacteriol. , vol.183 , pp. 5942-5955
    • Epple, U.D.1    Suriapranata, I.2    Eskelinen, E.L.3    Thumm, M.4
  • 111
    • 33947369047 scopus 로고    scopus 로고
    • Permeases recycle amino acids resulting from autophagy
    • Yang Z., and Klionsky D.J. Permeases recycle amino acids resulting from autophagy. Autophagy 3 (2007) 149-150
    • (2007) Autophagy , vol.3 , pp. 149-150
    • Yang, Z.1    Klionsky, D.J.2


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