메뉴 건너뛰기




Volumn 1853, Issue 10, 2015, Pages 2756-2765

Mitophagy in yeast: Molecular mechanisms and physiological role

Author keywords

Atg32; Autophagy; ERMES; Mitochondrion; Mitophagy; Yeast

Indexed keywords

ADAPTOR PROTEIN; ATG11 PROTEIN; ATG19 PROTEIN; ATG32 PROTEIN; ATG34 PROTEIN; ATG8 PROTEIN; CASEIN KINASE II; CYTOCHROME C; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE HOG1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE SLT2; OUTER MEMBRANE PROTEIN; PERMETHRIN; PHOSPHOPROTEIN PHOSPHATASE; PPATG30 PROTEIN; PROTEIN SERINE THREONINE KINASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; RECEPTOR PROTEIN; SERINE; THREONINE; THYMOCYTE ANTIBODY; UBIQUITIN; UBIQUITINATED PROTEIN; UNCLASSIFIED DRUG; ATG32 PROTEIN, S CEREVISIAE; CELL RECEPTOR; REACTIVE OXYGEN METABOLITE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84940721729     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.01.005     Document Type: Review
Times cited : (85)

References (137)
  • 2
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: a history of macroautophagy
    • Yang Z., Klionsky D.J. Eaten alive: a history of macroautophagy. Nat. Cell Biol. 2010, 12:814-822.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 3
    • 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. 1998, 273:21883-21892.
    • (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
  • 4
    • 0025363276 scopus 로고
    • Studies on the mechanisms of autophagy: formation of the autophagic vacuole
    • Dunn W.A. Studies on the mechanisms of autophagy: formation of the autophagic vacuole. J. Cell Biol. 1990, 110:1923-1933.
    • (1990) J. Cell Biol. , vol.110 , pp. 1923-1933
    • Dunn, W.A.1
  • 6
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B., Mizushima N., Virgin H.W. Autophagy in immunity and inflammation. Nature 2011, 469:323-335.
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 7
    • 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 2008, 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 8
    • 84877628647 scopus 로고    scopus 로고
    • Autophagy in human health and disease
    • Choi A.M., Ryter S.W., Levine B. Autophagy in human health and disease. N. Engl. J. Med. 2013, 368:651-662.
    • (2013) N. Engl. J. Med. , vol.368 , pp. 651-662
    • Choi, A.M.1    Ryter, S.W.2    Levine, B.3
  • 9
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006, 443:780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 10
    • 84871002139 scopus 로고    scopus 로고
    • Selective autophagy in budding yeast
    • Suzuki K. Selective autophagy in budding yeast. Cell Death Differ. 2013, 20:43-48.
    • (2013) Cell Death Differ. , vol.20 , pp. 43-48
    • Suzuki, K.1
  • 11
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters J.J. Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res. 2005, 8:3-5.
    • (2005) Rejuvenation Res. , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 12
    • 0032145866 scopus 로고    scopus 로고
    • Delivery of proteins and organelles to the vacuole from the cytoplasm
    • Scott S.V., Klionsky D.J. Delivery of proteins and organelles to the vacuole from the cytoplasm. Curr. Opin. Cell Biol. 1998, 10:523-529.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 523-529
    • Scott, S.V.1    Klionsky, D.J.2
  • 13
    • 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., Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell Biol. 2008, 10:602-610.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 14
    • 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 2007, 3:285-287.
    • (2007) Autophagy , vol.3 , pp. 285-287
    • Bernales, S.1    Schuck, S.2    Walter, P.3
  • 16
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding W.X., Ni H.M., Gao W., Yoshimori T., Stolz D.B., Ron D., Yin X.M. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am. J. Pathol. 2007, 171:513-524.
    • (2007) Am. J. Pathol. , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6    Yin, X.M.7
  • 18
    • 12944308330 scopus 로고    scopus 로고
    • Eating oneself and uninvited guests: autophagy-related pathways in cellular defense
    • Levine B. Eating oneself and uninvited guests: autophagy-related pathways in cellular defense. Cell 2005, 120:159-162.
    • (2005) Cell , vol.120 , pp. 159-162
    • Levine, B.1
  • 19
    • 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., Klionsky D.J. Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J. Cell Biol. 1995, 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
  • 20
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada M., Ohsumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 1993, 333:169-174.
    • (1993) FEBS Lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 22
    • 0029953575 scopus 로고    scopus 로고
    • Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway
    • Harding T.M., Hefner-Gravink A., Thumm M., Klionsky D.J. Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway. J. Biol. Chem. 1996, 271:17621-17624.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17621-17624
    • Harding, T.M.1    Hefner-Gravink, A.2    Thumm, M.3    Klionsky, D.J.4
  • 23
    • 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., Dunn W.A. Glucose-induced microautophagy in Pichia pastoris requires the alpha-subunit of phosphofructokinase. J. Cell Sci. 1997, 110(Pt 16):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    Dunn, W.A.5
  • 24
    • 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.K., Keller G.A., Subramani S. Peroxisome degradation by microautophagy in Pichia pastoris: identification of specific steps and morphological intermediates. J. Cell Biol. 1998, 141:625-636.
    • (1998) J. Cell Biol. , vol.141 , pp. 625-636
    • Sakai, Y.1    Koller, A.2    Rangell, L.K.3    Keller, G.A.4    Subramani, S.5
  • 26
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 2005, 39:359-407.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 27
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota D.A., Davies K.J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 2002, 4:674-680.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 28
    • 67650091290 scopus 로고    scopus 로고
    • Increasing organismal healthspan by enhancing mitochondrial protein quality control
    • Luce K., Osiewacz H.D. Increasing organismal healthspan by enhancing mitochondrial protein quality control. Nat. Cell Biol. 2009, 11:852-858.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 852-858
    • Luce, K.1    Osiewacz, H.D.2
  • 29
    • 76849100919 scopus 로고    scopus 로고
    • The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans
    • Haynes C.M., Yang Y., Blais S.P., Neubert T.A., Ron D. The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans. Mol. Cell 2010, 37:529-540.
    • (2010) Mol. Cell , vol.37 , pp. 529-540
    • Haynes, C.M.1    Yang, Y.2    Blais, S.P.3    Neubert, T.A.4    Ron, D.5
  • 30
    • 84907429451 scopus 로고    scopus 로고
    • Formation and repair of oxidative damage in the mitochondrial DNA
    • Muftuoglu M., Mori M.P., de Souza-Pinto N.C. Formation and repair of oxidative damage in the mitochondrial DNA. Mitochondrion 2014, 17:164-181.
    • (2014) Mitochondrion , vol.17 , pp. 164-181
    • Muftuoglu, M.1    Mori, M.P.2    de Souza-Pinto, N.C.3
  • 33
    • 84856244072 scopus 로고    scopus 로고
    • Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast
    • Kurihara Y., Kanki T., Aoki Y., Hirota Y., Saigusa T., Uchiumi T., Kang D. Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast. J. Biol. Chem. 2012, 287:3265-3272.
    • (2012) J. Biol. Chem. , vol.287 , pp. 3265-3272
    • Kurihara, Y.1    Kanki, T.2    Aoki, Y.3    Hirota, Y.4    Saigusa, T.5    Uchiumi, T.6    Kang, D.7
  • 34
    • 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. 2008, 183:795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 43
    • 84908065760 scopus 로고    scopus 로고
    • Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
    • Wong Y.C., Holzbaur E.L. Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation. Proc. Natl. Acad. Sci. U. S. A. 2014, 111:E4439-E4448.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. E4439-E4448
    • Wong, Y.C.1    Holzbaur, E.L.2
  • 46
    • 84901615924 scopus 로고    scopus 로고
    • PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix
    • Thomas R.E., Andrews L.A., Burman J.L., Lin W.Y., Pallanck L.J. PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix. Plos Genet. 2014, 10:e1004279.
    • (2014) Plos Genet. , vol.10 , pp. e1004279
    • Thomas, R.E.1    Andrews, L.A.2    Burman, J.L.3    Lin, W.Y.4    Pallanck, L.J.5
  • 47
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathway
    • Yamano K., Youle R.J. PINK1 is degraded through the N-end rule pathway. Autophagy 2013, 9:1758-1769.
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 49
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E., Tao R.N., Whitworth A.J. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:5018-5023.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 50
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/Parkin pathway
    • Poole A.C., Thomas R.E., Yu S., Vincow E.S., Pallanck L. The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/Parkin pathway. Plos ONE 2010, 5.
    • (2010) Plos ONE , vol.5
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 52
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg M.E., Cooper J.M., Chau K.Y., Rojo M., Schapira A.H.V., Taanman J.W. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 2010, 19:4861-4870.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.V.5    Taanman, J.W.6
  • 54
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells: revisiting a 40-year-old conundrum
    • Mijaljica D., Prescott M., Devenish R.J. Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy 2011, 7:673-682.
    • (2011) Autophagy , vol.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 55
    • 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. 2012, 22:407-417.
    • (2012) Trends Cell Biol. , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 56
  • 57
    • 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., Schweyen R.J. Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy. Cell Death Differ. 2007, 14:1647-1656.
    • (2007) Cell Death Differ. , vol.14 , pp. 1647-1656
    • Nowikovsky, K.1    Reipert, S.2    Devenish, R.J.3    Schweyen, R.J.4
  • 58
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T., Wang K., Cao Y., Baba M., Klionsky D.J. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev. Cell 2009, 17:98-109.
    • (2009) Dev. Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 59
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K., Kondo-Okamoto N., Ohsumi Y. Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev. Cell 2009, 17:87-97.
    • (2009) Dev. Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 60
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissova I., Deffieu M., Manon S., Camougrand N. Uth1p is involved in the autophagic degradation of mitochondria. J. Biol. Chem. 2004, 279:39068-39074.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 61
    • 57749121573 scopus 로고    scopus 로고
    • Mitophagy in yeast occurs through a selective mechanism
    • Kanki T., Klionsky D.J. Mitophagy in yeast occurs through a selective mechanism. J. Biol. Chem. 2008, 283:32386-32393.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32386-32393
    • Kanki, T.1    Klionsky, D.J.2
  • 62
    • 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., Abeliovich H. Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival. J. Biol. Chem. 2007, 282:5617-5624.
    • (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
  • 63
    • 34250811414 scopus 로고    scopus 로고
    • The role of autophagy in mitochondria maintenance: characterization of mitochondrial functions in autophagy-deficient S. cerevisiae strains
    • Zhang Y., Qi H., Taylor R., Xu W., Liu L.F., Jin S. The role of autophagy in mitochondria maintenance: characterization of mitochondrial functions in autophagy-deficient S. cerevisiae strains. Autophagy 2007, 3:337-346.
    • (2007) Autophagy , vol.3 , pp. 337-346
    • Zhang, Y.1    Qi, H.2    Taylor, R.3    Xu, W.4    Liu, L.F.5    Jin, S.6
  • 66
    • 0036901104 scopus 로고    scopus 로고
    • Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway
    • Shintani T., Huang W.P., Stromhaug P.E., Klionsky D.J. Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway. Dev. Cell 2002, 3:825-837.
    • (2002) Dev. Cell , vol.3 , pp. 825-837
    • Shintani, T.1    Huang, W.P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 67
    • 42049094041 scopus 로고    scopus 로고
    • PpAtg30 tags peroxisomes for turnover by selective autophagy
    • Farre J.C., Manjithaya R., Mathewson R.D., Subramani S. PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev. Cell 2008, 14:365-376.
    • (2008) Dev. Cell , vol.14 , pp. 365-376
    • Farre, J.C.1    Manjithaya, R.2    Mathewson, R.D.3    Subramani, S.4
  • 68
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley A.M., Nuttall J.M., Hettema E.H. Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J. 2012, 31:2852-2868.
    • (2012) EMBO J. , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 71
    • 84887472941 scopus 로고    scopus 로고
    • Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy
    • Wang K., Jin M., Liu X., Klionsky D.J. Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy. Autophagy 2013, 9:1828-1836.
    • (2013) Autophagy , vol.9 , pp. 1828-1836
    • Wang, K.1    Jin, M.2    Liu, X.3    Klionsky, D.J.4
  • 73
    • 84877579321 scopus 로고    scopus 로고
    • Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11
    • Farre J.C., Burkenroad A., Burnett S.F., Subramani S. Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11. EMBO Rep. 2013, 14:441-449.
    • (2013) EMBO Rep. , vol.14 , pp. 441-449
    • Farre, J.C.1    Burkenroad, A.2    Burnett, S.F.3    Subramani, S.4
  • 76
    • 77956924900 scopus 로고    scopus 로고
    • Selective transport of alpha-mannosidase by autophagic pathways: identification of a novel receptor, Atg34p
    • Suzuki K., Kondo C., Morimoto M., Ohsumi Y. Selective transport of alpha-mannosidase by autophagic pathways: identification of a novel receptor, Atg34p. J. Biol. Chem. 2010, 285:30019-30025.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30019-30025
    • Suzuki, K.1    Kondo, C.2    Morimoto, M.3    Ohsumi, Y.4
  • 77
    • 84908227585 scopus 로고    scopus 로고
    • Hrr25 phosphorylates the autophagic receptor Atg34 to promote vacuolar transport of alpha-mannosidase under nitrogen starvation conditions
    • Mochida K., Ohsumi Y., Nakatogawa H. Hrr25 phosphorylates the autophagic receptor Atg34 to promote vacuolar transport of alpha-mannosidase under nitrogen starvation conditions. FEBS Lett. 2014, 588:3862-3869.
    • (2014) FEBS Lett. , vol.588 , pp. 3862-3869
    • Mochida, K.1    Ohsumi, Y.2    Nakatogawa, H.3
  • 79
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • Noda N.N., Ohsumi Y., Inagaki F. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett. 2010, 584:1379-1385.
    • (2010) FEBS Lett. , vol.584 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 80
    • 84903776410 scopus 로고    scopus 로고
    • Scaffolding the expansion of autophagosomes
    • Kaufmann A., Wollert T. Scaffolding the expansion of autophagosomes. Autophagy 2014, 10:1343-1345.
    • (2014) Autophagy , vol.10 , pp. 1343-1345
    • Kaufmann, A.1    Wollert, T.2
  • 81
    • 84893500894 scopus 로고    scopus 로고
    • Molecular mechanism of autophagic membrane-scaffold assembly and disassembly
    • Kaufmann A., Beier V., Franquelim H.G., Wollert T. Molecular mechanism of autophagic membrane-scaffold assembly and disassembly. Cell 2014, 156:469-481.
    • (2014) Cell , vol.156 , pp. 469-481
    • Kaufmann, A.1    Beier, V.2    Franquelim, H.G.3    Wollert, T.4
  • 82
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K., Shaw J.M. Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 2005, 39:503-536.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 83
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes L.C., Di Benedetto G., Scorrano L. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat. Cell Biol. 2011, 13:589-598.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 84
    • 79959987510 scopus 로고    scopus 로고
    • Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation
    • Rambold A.S., Kostelecky B., Elia N., Lippincott-Schwartz J. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:10190-10195.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 10190-10195
    • Rambold, A.S.1    Kostelecky, B.2    Elia, N.3    Lippincott-Schwartz, J.4
  • 89
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy A.D., McCaffery J.M., Shaw J.M. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 2000, 151:367-380.
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 90
    • 0034676101 scopus 로고    scopus 로고
    • Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division
    • Tieu Q., Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J. Cell Biol. 2000, 151:353-366.
    • (2000) J. Cell Biol. , vol.151 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 91
    • 22944440071 scopus 로고    scopus 로고
    • The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria
    • Griffin E.E., Graumann J., Chan D.C. The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria. J. Cell Biol. 2005, 170:237-248.
    • (2005) J. Cell Biol. , vol.170 , pp. 237-248
    • Griffin, E.E.1    Graumann, J.2    Chan, D.C.3
  • 92
    • 84880506979 scopus 로고    scopus 로고
    • The scaffold protein Atg11 recruits fission machinery to drive selective mitochondria degradation by autophagy
    • Mao K., Wang K., Liu X., Klionsky D.J. The scaffold protein Atg11 recruits fission machinery to drive selective mitochondria degradation by autophagy. Dev. Cell 2013, 26:9-18.
    • (2013) Dev. Cell , vol.26 , pp. 9-18
    • Mao, K.1    Wang, K.2    Liu, X.3    Klionsky, D.J.4
  • 93
    • 84888163960 scopus 로고    scopus 로고
    • Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy
    • Abeliovich H., Zarei M., Rigbolt K.T., Youle R.J., Dengjel J. Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy. Nat. Commun. 2013, 4:2789.
    • (2013) Nat. Commun. , vol.4 , pp. 2789
    • Abeliovich, H.1    Zarei, M.2    Rigbolt, K.T.3    Youle, R.J.4    Dengjel, J.5
  • 94
    • 79953158981 scopus 로고    scopus 로고
    • Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2
    • Mendl N., Occhipinti A., Muller M., Wild P., Dikic I., Reichert A.S. Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2. J. Cell Sci. 2011, 124:1339-1350.
    • (2011) J. Cell Sci. , vol.124 , pp. 1339-1350
    • Mendl, N.1    Occhipinti, A.2    Muller, M.3    Wild, P.4    Dikic, I.5    Reichert, A.S.6
  • 96
    • 84894326290 scopus 로고    scopus 로고
    • Mitochondrial ER contacts are crucial for mitophagy in yeast
    • Bockler S., Westermann B. Mitochondrial ER contacts are crucial for mitophagy in yeast. Dev. Cell 2014, 28:450-458.
    • (2014) Dev. Cell , vol.28 , pp. 450-458
    • Bockler, S.1    Westermann, B.2
  • 98
    • 84890925982 scopus 로고    scopus 로고
    • Bit-by-bit autophagic removal of parkin-labelled mitochondria
    • Yang J.Y., Yang W.Y. Bit-by-bit autophagic removal of parkin-labelled mitochondria. Nat. Commun. 2013, 4:2428.
    • (2013) Nat. Commun. , vol.4 , pp. 2428
    • Yang, J.Y.1    Yang, W.Y.2
  • 100
    • 72149110062 scopus 로고    scopus 로고
    • Aup1-mediated regulation of Rtg3 during mitophagy
    • Journo D., Mor A., Abeliovich H. Aup1-mediated regulation of Rtg3 during mitophagy. J. Biol. Chem. 2009, 284:35885-35895.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35885-35895
    • Journo, D.1    Mor, A.2    Abeliovich, H.3
  • 101
    • 84885327315 scopus 로고    scopus 로고
    • Uth1 is a mitochondrial inner membrane protein dispensable for post-log-phase and rapamycin-induced mitophagy
    • Welter E., Montino M., Reinhold R., Schlotterhose P., Krick R., Dudek J., Rehling P., Thumm M. Uth1 is a mitochondrial inner membrane protein dispensable for post-log-phase and rapamycin-induced mitophagy. FEBS J. 2013, 280:4970-4982.
    • (2013) FEBS J. , vol.280 , pp. 4970-4982
    • Welter, E.1    Montino, M.2    Reinhold, R.3    Schlotterhose, P.4    Krick, R.5    Dudek, J.6    Rehling, P.7    Thumm, M.8
  • 102
    • 84878780410 scopus 로고    scopus 로고
    • Mitochondrial degradation during starvation is selective and temporally distinct from bulk autophagy in yeast
    • Eiyama A., Kondo-Okamoto N., Okamoto K. Mitochondrial degradation during starvation is selective and temporally distinct from bulk autophagy in yeast. FEBS Lett. 2013, 587:1787-1792.
    • (2013) FEBS Lett. , vol.587 , pp. 1787-1792
    • Eiyama, A.1    Kondo-Okamoto, N.2    Okamoto, K.3
  • 103
    • 79958219318 scopus 로고    scopus 로고
    • Two MAPK-signaling pathways are required for mitophagy in Saccharomyces cerevisiae
    • Mao K., Wang K., Zhao M., Xu T., Klionsky D.J. Two MAPK-signaling pathways are required for mitophagy in Saccharomyces cerevisiae. J. Cell Biol. 2011, 193:755-767.
    • (2011) J. Cell Biol. , vol.193 , pp. 755-767
    • Mao, K.1    Wang, K.2    Zhao, M.3    Xu, T.4    Klionsky, D.J.5
  • 104
    • 20544432791 scopus 로고    scopus 로고
    • Cell wall integrity signaling in Saccharomyces cerevisiae
    • Levin D.E. Cell wall integrity signaling in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 2005, 69:262-291.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 262-291
    • Levin, D.E.1
  • 105
    • 4644278405 scopus 로고    scopus 로고
    • MAPK signaling: Sho business
    • Seet B.T., Pawson T. MAPK signaling: Sho business. Curr. Biol. 2004, 14:R708-R710.
    • (2004) Curr. Biol. , vol.14 , pp. R708-R710
    • Seet, B.T.1    Pawson, T.2
  • 108
    • 0035794147 scopus 로고    scopus 로고
    • Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions
    • Lefebvre-Legendre L., Vaillier J., Benabdelhak H., Velours J., Slonimski P.P., di Rago J.P. Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions. J. Biol. Chem. 2001, 276:6789-6796.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6789-6796
    • Lefebvre-Legendre, L.1    Vaillier, J.2    Benabdelhak, H.3    Velours, J.4    Slonimski, P.P.5    di Rago, J.P.6
  • 110
    • 80052631022 scopus 로고    scopus 로고
    • Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane
    • Lupo D., Vollmer C., Deckers M., Mick D.U., Tews I., Sinning I., Rehling P. Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane. Traffic 2011, 12:1457-1466.
    • (2011) Traffic , vol.12 , pp. 1457-1466
    • Lupo, D.1    Vollmer, C.2    Deckers, M.3    Mick, D.U.4    Tews, I.5    Sinning, I.6    Rehling, P.7
  • 112
    • 19444366152 scopus 로고    scopus 로고
    • Electroneutral K+/H+ exchange in mitochondrial membrane vesicles involves Yol027/Letm1 proteins
    • Froschauer E., Nowikovsky K., Schweyen R.J. Electroneutral K+/H+ exchange in mitochondrial membrane vesicles involves Yol027/Letm1 proteins. Biochim. Biophys. Acta 2005, 1711:41-48.
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 41-48
    • Froschauer, E.1    Nowikovsky, K.2    Schweyen, R.J.3
  • 113
    • 70349669093 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter
    • Jiang D.W., Zhao L.L., Clapham D.E. Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter. Science 2009, 326:144-147.
    • (2009) Science , vol.326 , pp. 144-147
    • Jiang, D.W.1    Zhao, L.L.2    Clapham, D.E.3
  • 116
    • 84940718214 scopus 로고    scopus 로고
    • Mitophagy is primarily due to alternative autophagy and requires the MAPK1 and MAPK14 signaling pathways
    • (in press)
    • Hirota Y., Yamashita S., Kurihara Y., Jin X., Aihara M., Saigusa T., Kang D., Kanki T. Mitophagy is primarily due to alternative autophagy and requires the MAPK1 and MAPK14 signaling pathways. Autophagy 2015, (in press).
    • (2015) Autophagy
    • Hirota, Y.1    Yamashita, S.2    Kurihara, Y.3    Jin, X.4    Aihara, M.5    Saigusa, T.6    Kang, D.7    Kanki, T.8
  • 117
    • 0035839430 scopus 로고    scopus 로고
    • Apg2 is a novel protein required for the cytoplasm to vacuole targeting, autophagy, and pexophagy pathways
    • Wang C.W., Kim J., Huang W.P., Abeliovich H., Stromhaug P.E., Dunn W.A., Klionsky D.J. Apg2 is a novel protein required for the cytoplasm to vacuole targeting, autophagy, and pexophagy pathways. J. Biol. Chem. 2001, 276:30442-30451.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30442-30451
    • Wang, C.W.1    Kim, J.2    Huang, W.P.3    Abeliovich, H.4    Stromhaug, P.E.5    Dunn, W.A.6    Klionsky, D.J.7
  • 118
    • 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., Klionsky D.J. Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways. Mol. Biol. Cell 1999, 10:1337-1351.
    • (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
  • 119
    • 0347611578 scopus 로고    scopus 로고
    • Atg23 is essential for the cytoplasm to vacuole targeting pathway and efficient autophagy but not pexophagy
    • Tucker K.A., Reggiori F., Dunn W.A., Klionsky D.J. Atg23 is essential for the cytoplasm to vacuole targeting pathway and efficient autophagy but not pexophagy. J. Biol. Chem. 2003, 278:48445-48452.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48445-48452
    • Tucker, K.A.1    Reggiori, F.2    Dunn, W.A.3    Klionsky, D.J.4
  • 120
    • 0037424491 scopus 로고    scopus 로고
    • Intravacuolar membrane lysis in Saccharomyces cerevisiae. Does vacuolar targeting of Cvt17/Aut5p affect its function?
    • Epple U.D., Eskelinen E.L., Thumm M. Intravacuolar membrane lysis in Saccharomyces cerevisiae. Does vacuolar targeting of Cvt17/Aut5p affect its function?. J. Biol. Chem. 2003, 278:7810-7821.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7810-7821
    • Epple, U.D.1    Eskelinen, E.L.2    Thumm, M.3
  • 121
    • 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., Thumm M. Aut5/Cvt17p, a putative lipase essential for disintegration of autophagic bodies inside the vacuole. J. Bacteriol. 2001, 183:5942-5955.
    • (2001) J. Bacteriol. , vol.183 , pp. 5942-5955
    • Epple, U.D.1    Suriapranata, I.2    Eskelinen, E.L.3    Thumm, M.4
  • 122
    • 0035910577 scopus 로고    scopus 로고
    • Degradation of lipid vesicles in the yeast vacuole requires function of Cvt17, a putative lipase
    • Teter S.A., Eggerton K.P., Scott S.V., Kim J., Fischer A.M., Klionsky D.J. Degradation of lipid vesicles in the yeast vacuole requires function of Cvt17, a putative lipase. J. Biol. Chem. 2001, 276:2083-2087.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2083-2087
    • Teter, S.A.1    Eggerton, K.P.2    Scott, S.V.3    Kim, J.4    Fischer, A.M.5    Klionsky, D.J.6
  • 126
    • 0035834395 scopus 로고    scopus 로고
    • Autophagy and the cytoplasm to vacuole targeting pathway both require Aut10p
    • Barth H., Meiling-Wesse K., Epple U.D., Thumm M. Autophagy and the cytoplasm to vacuole targeting pathway both require Aut10p. FEBS Lett. 2001, 508:23-28.
    • (2001) FEBS Lett. , vol.508 , pp. 23-28
    • Barth, H.1    Meiling-Wesse, K.2    Epple, U.D.3    Thumm, M.4
  • 127
    • 0035661648 scopus 로고    scopus 로고
    • Cvt18/Gsa12 is required for cytoplasm-to-vacuole transport, pexophagy, and autophagy in Saccharomyces cerevisiae and Pichia pastoris
    • Guan J., Stromhaug P.E., George M.D., Habibzadegah-Tari P., Bevan A., Dunn W.A., Klionsky D.J. Cvt18/Gsa12 is required for cytoplasm-to-vacuole transport, pexophagy, and autophagy in Saccharomyces cerevisiae and Pichia pastoris. Mol. Biol. Cell 2001, 12:3821-3838.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3821-3838
    • Guan, J.1    Stromhaug, P.E.2    George, M.D.3    Habibzadegah-Tari, P.4    Bevan, A.5    Dunn, W.A.6    Klionsky, D.J.7
  • 128
    • 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., Klionsky D.J. Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway. Mol. Cell 2001, 7:1131-1141.
    • (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
  • 129
    • 0037119448 scopus 로고    scopus 로고
    • Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy
    • Nice D.C., Sato T.K., Stromhaug P.E., Emr S.D., Klionsky D.J. Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy. J. Biol. Chem. 2002, 277:30198-30207.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30198-30207
    • Nice, D.C.1    Sato, T.K.2    Stromhaug, P.E.3    Emr, S.D.4    Klionsky, D.J.5
  • 130
    • 0037070221 scopus 로고    scopus 로고
    • Mai1p is essential for maturation of proaminopeptidase I but not for autophagy
    • Barth H., Meiling-Wesse K., Epple U.D., Thumm M. Mai1p is essential for maturation of proaminopeptidase I but not for autophagy. FEBS Lett. 2002, 512:173-179.
    • (2002) FEBS Lett. , vol.512 , pp. 173-179
    • Barth, H.1    Meiling-Wesse, K.2    Epple, U.D.3    Thumm, M.4
  • 131
    • 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., Klionsky D.J. Atg22 recycles amino acids to link the degradative and recycling functions of autophagy. Mol. Biol. Cell 2006, 17:5094-5104.
    • (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
  • 132
    • 33846140410 scopus 로고    scopus 로고
    • Atg26 is not involved in autophagy-related pathways in Saccharomyces cerevisiae
    • Cao Y., Klionsky D.J. Atg26 is not involved in autophagy-related pathways in Saccharomyces cerevisiae. Autophagy 2007, 3:17-20.
    • (2007) Autophagy , vol.3 , pp. 17-20
    • Cao, Y.1    Klionsky, D.J.2
  • 133
    • 0037135980 scopus 로고    scopus 로고
    • Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy
    • Wurmser A.E., Emr S.D. Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy. J. Cell Biol. 2002, 158:761-772.
    • (2002) J. Cell Biol. , vol.158 , pp. 761-772
    • Wurmser, A.E.1    Emr, S.D.2
  • 134
    • 33846807374 scopus 로고    scopus 로고
    • Atg27 is required for autophagy-dependent cycling of Atg9
    • Yen W.L., Legakis J.E., Nair U., Klionsky D.J. Atg27 is required for autophagy-dependent cycling of Atg9. Mol. Biol. Cell 2007, 18:581-593.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 581-593
    • Yen, W.L.1    Legakis, J.E.2    Nair, U.3    Klionsky, D.J.4
  • 136
    • 33947378818 scopus 로고    scopus 로고
    • Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae
    • Kabeya Y., Kawamata T., Suzuki K., Ohsumi Y. Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 2007, 356:405-410.
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 405-410
    • Kabeya, Y.1    Kawamata, T.2    Suzuki, K.3    Ohsumi, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.