메뉴 건너뛰기




Volumn 1853, Issue 10, 2015, Pages 2766-2774

Mitophagy and mitochondrial dynamics in Saccharomyces cerevisiae

Author keywords

Atg32; Dnm1; Mgm1; Mitochondrial dynamics; Mitophagy; Ubiquitination

Indexed keywords

IRON; SULFUR;

EID: 84940718398     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.02.024     Document Type: Review
Times cited : (33)

References (119)
  • 1
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 2003, 112:481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 2
    • 52049104467 scopus 로고    scopus 로고
    • The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
    • Drose S., Brandt U. The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex. J. Biol. Chem. 2008, 283:21649-21654.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21649-21654
    • Drose, S.1    Brandt, U.2
  • 3
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 2007, 87:99-163.
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 4
    • 0345010008 scopus 로고
    • An electron microscope study of the mitochondrial structure
    • Palade G.E. An electron microscope study of the mitochondrial structure. J. Histochem. Cytochem. 1953, 1:188-211.
    • (1953) J. Histochem. Cytochem. , vol.1 , pp. 188-211
    • Palade, G.E.1
  • 5
    • 0031081742 scopus 로고    scopus 로고
    • Reconsidering mitochondrial structure: new views of an old organelle
    • Mannella C.A., Marko M., Buttle K. Reconsidering mitochondrial structure: new views of an old organelle. Trends Biochem. Sci. 1997, 22:37-38.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 37-38
    • Mannella, C.A.1    Marko, M.2    Buttle, K.3
  • 6
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey T.G., Mannella C.A. The internal structure of mitochondria. Trends Biochem. Sci. 2000, 25:319-324.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 7
    • 67649321228 scopus 로고    scopus 로고
    • Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion
    • Zick M., Duvezin-Caubet S., Schafer A., Vogel F., Neupert W., Reichert A.S. Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion. FEBS Lett. 2009, 583:2237-2243.
    • (2009) FEBS Lett. , vol.583 , pp. 2237-2243
    • Zick, M.1    Duvezin-Caubet, S.2    Schafer, A.3    Vogel, F.4    Neupert, W.5    Reichert, A.S.6
  • 8
    • 0037055983 scopus 로고    scopus 로고
    • Insight into mitochondrial structure and function from electron tomography
    • Frey T.G., Renken C.W., Perkins G.A. Insight into mitochondrial structure and function from electron tomography. Biochim. Biophys. Acta 2002, 1555:196-203.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 196-203
    • Frey, T.G.1    Renken, C.W.2    Perkins, G.A.3
  • 9
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel F., Bornhövd C., Neupert W., Reichert A.S. Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 2006, 175:237-247.
    • (2006) J. Cell Biol. , vol.175 , pp. 237-247
    • Vogel, F.1    Bornhövd, C.2    Neupert, W.3    Reichert, A.S.4
  • 10
    • 33745737928 scopus 로고    scopus 로고
    • Structure and dynamics of the mitochondrial inner membrane cristae
    • Mannella C.A. Structure and dynamics of the mitochondrial inner membrane cristae. Biochim. Biophys. Acta 2006, 1763:542-548.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 542-548
    • Mannella, C.A.1
  • 11
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
    • Wurm C.A., Jakobs S. Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast. FEBS Lett. 2006, 580:5628-5634.
    • (2006) FEBS Lett. , vol.580 , pp. 5628-5634
    • Wurm, C.A.1    Jakobs, S.2
  • 12
    • 0029610067 scopus 로고
    • Uniparental inheritance of mitochondrial and chloroplast genes: mechanisms and evolution
    • Birky C.W. Uniparental inheritance of mitochondrial and chloroplast genes: mechanisms and evolution. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:11331-11338.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11331-11338
    • Birky, C.W.1
  • 14
    • 0033561361 scopus 로고    scopus 로고
    • Animal mitochondrial genomes
    • Boore J.L. Animal mitochondrial genomes. Nucleic Acids Res. 1999, 27:1767-1780.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1767-1780
    • Boore, J.L.1
  • 15
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: from proteomics to functional mechanisms
    • Schmidt O., Pfanner N., Meisinger C. Mitochondrial protein import: from proteomics to functional mechanisms. Nat. Rev. Mol. Cell Biol. 2010, 11:655-667.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 16
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 2007, 76:723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 17
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Chen H., Chan D.C. Emerging functions of mammalian mitochondrial fusion and fission. Hum. Mol. Genet. 2005, 14(2):R283-R289.
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.2 , pp. R283-R289
    • Chen, H.1    Chan, D.C.2
  • 18
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari J., Marshall W.F., Straight A., Murray A., Sedat J.W., Walter P. Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 1997, 8:1233-1242.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 20
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li Z., Okamoto K., Hayashi Y., Sheng M. The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 2004, 119:873-887.
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 21
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S., Lackner L., Nunnari J. The machines that divide and fuse mitochondria. Annu. Rev. Biochem. 2007, 76:751-780.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 22
    • 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
  • 23
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann B. Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol. 2010, 11:872-884.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 872-884
    • Westermann, B.1
  • 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
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria: in sickness and in health
    • Nunnari J., Suomalainen A. Mitochondria: in sickness and in health. Cell 2012, 148:1145-1159.
    • (2012) Cell , vol.148 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 28
    • 84903135154 scopus 로고    scopus 로고
    • MtDNA mutations and their role in aging, diseases and forensic sciences
    • Zapico S.C., Ubelaker D.H. MtDNA mutations and their role in aging, diseases and forensic sciences. Aging Dis. 2013, 4:364-380.
    • (2013) Aging Dis. , vol.4 , pp. 364-380
    • Zapico, S.C.1    Ubelaker, D.H.2
  • 30
    • 70349437277 scopus 로고    scopus 로고
    • Emerging roles of mitochondrial membrane dynamics in health and disease
    • Schäfer A., Reichert A.S. Emerging roles of mitochondrial membrane dynamics in health and disease. Biol. Chem. 2009, 390:707-715.
    • (2009) Biol. Chem. , vol.390 , pp. 707-715
    • Schäfer, A.1    Reichert, A.S.2
  • 33
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: protection against neurodegeneration and ageing
    • Tatsuta T., Langer T. Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J. 2008, 27:306-314.
    • (2008) EMBO J. , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 34
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases
    • Koppen M., Langer T. Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases. Crit. Rev. Biochem. Mol. Biol. 2007, 42:221-242.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 221-242
    • Koppen, M.1    Langer, T.2
  • 35
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
    • Nakada K., Inoue K., Ono T., Isobe K., Ogura A., Goto Y.I., Nonaka I., Hayashi J.I. Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat. Med. 2001, 7:934-940.
    • (2001) Nat. Med. , vol.7 , pp. 934-940
    • Nakada, K.1    Inoue, K.2    Ono, T.3    Isobe, K.4    Ogura, A.5    Goto, Y.I.6    Nonaka, I.7    Hayashi, J.I.8
  • 38
    • 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
  • 39
    • 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
  • 40
    • 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
  • 42
    • 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
  • 44
    • 84871005673 scopus 로고    scopus 로고
    • The pathways of mitophagy for quality control and clearance of mitochondria
    • Ashrafi G., Schwarz T.L. The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differ. 2013, 20:31-42.
    • (2013) Cell Death Differ. , vol.20 , pp. 31-42
    • Ashrafi, G.1    Schwarz, T.L.2
  • 45
    • 2142710081 scopus 로고    scopus 로고
    • Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor
    • Herlan M., Bornhovd C., Hell K., Neupert W., Reichert A.S. Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 2004, 165:167-173.
    • (2004) J. Cell Biol. , vol.165 , pp. 167-173
    • Herlan, M.1    Bornhovd, C.2    Hell, K.3    Neupert, W.4    Reichert, A.S.5
  • 46
    • 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
  • 47
  • 48
    • 79957923566 scopus 로고    scopus 로고
    • Mitochondria regulate autophagy by conserved signalling pathways
    • Graef M., Nunnari J. Mitochondria regulate autophagy by conserved signalling pathways. EMBO J. 2011, 30:2101-2114.
    • (2011) EMBO J. , vol.30 , pp. 2101-2114
    • Graef, M.1    Nunnari, J.2
  • 51
  • 53
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: from phenomenology to molecular understanding in less than a decade
    • Klionsky D.J. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 2007, 8:931-937.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 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
    • 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
  • 57
    • 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
  • 58
    • 0030852279 scopus 로고    scopus 로고
    • Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism
    • Scott S.V., Baba M., Ohsumi Y., Klionsky D.J. Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism. J. Cell Biol. 1997, 138:37-44.
    • (1997) J. Cell Biol. , vol.138 , pp. 37-44
    • Scott, S.V.1    Baba, M.2    Ohsumi, Y.3    Klionsky, D.J.4
  • 61
    • 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
  • 62
    • 0032847274 scopus 로고    scopus 로고
    • TOR kinase homologs function in a signal transduction pathway that is conserved from yeast to mammals
    • Cutler N.S., Heitman J., Cardenas M.E. TOR kinase homologs function in a signal transduction pathway that is conserved from yeast to mammals. Mol. Cell. Endocrinol. 1999, 155:135-142.
    • (1999) Mol. Cell. Endocrinol. , vol.155 , pp. 135-142
    • Cutler, N.S.1    Heitman, J.2    Cardenas, M.E.3
  • 63
    • 53849119118 scopus 로고    scopus 로고
    • Growth control via TOR kinase signaling, an intracellular sensor of amino acid and energy availability, with crosstalk potential to proline metabolism
    • Liao X.H., Majithia A., Huang X., Kimmel A.R. Growth control via TOR kinase signaling, an intracellular sensor of amino acid and energy availability, with crosstalk potential to proline metabolism. Amino Acids 2008, 35:761-770.
    • (2008) Amino Acids , vol.35 , pp. 761-770
    • Liao, X.H.1    Majithia, A.2    Huang, X.3    Kimmel, A.R.4
  • 64
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • Noda T., Ohsumi Y. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 1998, 273:3963-3966.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 65
    • 69349096593 scopus 로고    scopus 로고
    • Regulation of autophagy in yeast Saccharomyces cerevisiae
    • Cebollero E., Reggiori F. Regulation of autophagy in yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 2009, 1793:1413-1421.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1413-1421
    • Cebollero, E.1    Reggiori, F.2
  • 66
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman J., Movva N.R., Hall M.N. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science 1991, 253:905-909.
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 67
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S., Loewith R., Hall M.N. TOR signaling in growth and metabolism. Cell 2006, 124:471-484.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 70
    • 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., Jiang X. ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagy. J. Biol. Chem. 2009, 284:12297-12305.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    Lam du, H.2    Wang, J.3    Ding, X.4    Chen, S.5    Jiang, X.6
  • 71
    • 34948828483 scopus 로고    scopus 로고
    • Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae
    • Yorimitsu T., Zaman S., Broach J.R., Klionsky D.J. Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae. Mol. Biol. Cell 2007, 18:4180-4189.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4180-4189
    • Yorimitsu, T.1    Zaman, S.2    Broach, J.R.3    Klionsky, D.J.4
  • 72
    • 2442645050 scopus 로고    scopus 로고
    • The Ras/cAMP-dependent protein kinase signaling pathway regulates an early step of the autophagy process in Saccharomyces cerevisiae
    • Budovskaya Y.V., Stephan J.S., Reggiori F., Klionsky D.J., Herman P.K. The Ras/cAMP-dependent protein kinase signaling pathway regulates an early step of the autophagy process in Saccharomyces cerevisiae. J. Biol. Chem. 2004, 279:20663-20671.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20663-20671
    • Budovskaya, Y.V.1    Stephan, J.S.2    Reggiori, F.3    Klionsky, D.J.4    Herman, P.K.5
  • 73
    • 76449083770 scopus 로고    scopus 로고
    • The molecular mechanism of mitochondria autophagy in yeast
    • Kanki T., Klionsky D.J. The molecular mechanism of mitochondria autophagy in yeast. Mol. Microbiol. 2010, 75:795-800.
    • (2010) Mol. Microbiol. , vol.75 , pp. 795-800
    • Kanki, T.1    Klionsky, D.J.2
  • 74
    • 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
  • 75
    • 79953158981 scopus 로고    scopus 로고
    • Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2
    • Mendl N., Occhipinti A., Müller 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    Müller, M.3    Wild, P.4    Dikic, I.5    Reichert, A.S.6
  • 76
    • 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., 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.5    Taanman, J.W.6
  • 87
    • 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
  • 89
    • 84903817207 scopus 로고    scopus 로고
    • Receptor-mediated mitophagy in yeast and mammalian systems
    • Liu L., Sakakibara K., Chen Q., Okamoto K. Receptor-mediated mitophagy in yeast and mammalian systems. Cell Res. 2014, 24:787-795.
    • (2014) Cell Res. , vol.24 , pp. 787-795
    • Liu, L.1    Sakakibara, K.2    Chen, Q.3    Okamoto, K.4
  • 91
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige K., Baba M., Tsuboi S., Noda T., Ohsumi Y. Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 1992, 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
  • 93
    • 0031694197 scopus 로고    scopus 로고
    • Escape of mitochondrial DNA to the nucleus in yme1 yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments
    • Campbell C.L., Thorsness P.E. Escape of mitochondrial DNA to the nucleus in yme1 yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments. J. Cell Sci. 1998, 111(Pt 16):2455-2464.
    • (1998) J. Cell Sci. , vol.111 , pp. 2455-2464
    • Campbell, C.L.1    Thorsness, P.E.2
  • 94
    • 0029036915 scopus 로고
    • Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae
    • Noda T., Matsuura A., Wada Y., Ohsumi Y. Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 1995, 210:126-132.
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 126-132
    • Noda, T.1    Matsuura, A.2    Wada, Y.3    Ohsumi, Y.4
  • 98
    • 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
  • 100
    • 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
  • 101
    • 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
  • 102
    • 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
  • 103
    • 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
  • 104
    • 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
  • 106
    • 84861082440 scopus 로고    scopus 로고
    • The many faces of mitochondrial autophagy: making sense of contrasting observations in recent research
    • May A.I., Devenish R.J., Prescott M. The many faces of mitochondrial autophagy: making sense of contrasting observations in recent research. Int. J. Cell Biol. 2012, 2012:431684.
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 431684
    • May, A.I.1    Devenish, R.J.2    Prescott, M.3
  • 107
    • 0032478067 scopus 로고    scopus 로고
    • The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo
    • George R., Beddoe T., Landl K., Lithgow T. The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:2296-2301.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2296-2301
    • George, R.1    Beddoe, T.2    Landl, K.3    Lithgow, T.4
  • 108
    • 84894326290 scopus 로고    scopus 로고
    • Mitochondrial ER contacts are crucial for mitophagy in yeast
    • Böckler 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
    • Böckler, S.1    Westermann, B.2
  • 109
    • 0035998264 scopus 로고    scopus 로고
    • Yeast Whi2 and Psr1-phosphatase form a complex and regulate STRE-mediated gene expression
    • Kaida D., Yashiroda H., Toh-e A., Kikuchi Y. Yeast Whi2 and Psr1-phosphatase form a complex and regulate STRE-mediated gene expression. Genes Cells 2002, 7:543-552.
    • (2002) Genes Cells , vol.7 , pp. 543-552
    • Kaida, D.1    Yashiroda, H.2    Toh-e, A.3    Kikuchi, Y.4
  • 110
    • 80053379961 scopus 로고    scopus 로고
    • Mitophagy, mitochondrial dynamics and the general stress response in yeast
    • Müller M., Reichert A.S. Mitophagy, mitochondrial dynamics and the general stress response in yeast. Biochem. Soc. Trans. 2011, 39:1514-1519.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1514-1519
    • Müller, M.1    Reichert, A.S.2
  • 111
    • 0037415638 scopus 로고    scopus 로고
    • The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
    • Wong E.D., Wagner J.A., Scott S.V., Okreglak V., Holewinske T.J., Cassidy-Stone A., Nunnari J. The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. J. Cell Biol. 2003, 160:303-311.
    • (2003) J. Cell Biol. , vol.160 , pp. 303-311
    • Wong, E.D.1    Wagner, J.A.2    Scott, S.V.3    Okreglak, V.4    Holewinske, T.J.5    Cassidy-Stone, A.6    Nunnari, J.7
  • 112
    • 0034676095 scopus 로고    scopus 로고
    • The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria
    • Wong E.D., Wagner J.A., Gorsich S.W., McCaffery J.M., Shaw J.M., Nunnari J. The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria. J. Cell Biol. 2000, 151:341-352.
    • (2000) J. Cell Biol. , vol.151 , pp. 341-352
    • Wong, E.D.1    Wagner, J.A.2    Gorsich, S.W.3    McCaffery, J.M.4    Shaw, J.M.5    Nunnari, J.6
  • 113
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan M., Vogel F., Bornhovd C., Neupert W., Reichert A.S. Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 2003, 278:27781-27788.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhovd, C.3    Neupert, W.4    Reichert, A.S.5
  • 114
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban G.A., Saurya S., Freeman M. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 2003, 423:537-541.
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 115
    • 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
  • 116
    • 84865536459 scopus 로고    scopus 로고
    • The mitochondrial Dnm1-like fission component is required for lgA2-induced mitophagy but dispensable for starvation-induced mitophagy in Ustilago maydis
    • Nieto-Jacobo F., Pasch D., Basse C.W. The mitochondrial Dnm1-like fission component is required for lgA2-induced mitophagy but dispensable for starvation-induced mitophagy in Ustilago maydis. Eukaryot. Cell 2012, 11:1154-1166.
    • (2012) Eukaryot. Cell , vol.11 , pp. 1154-1166
    • Nieto-Jacobo, F.1    Pasch, D.2    Basse, C.W.3
  • 117
    • 84924614087 scopus 로고    scopus 로고
    • Synthetic Quantitative Array technology identifies the Ubp3-Bre5 deubiquitinase complex as a negative regulator of mitophagy
    • (Published online February 19, 2015)
    • Müller M., Kötter P., Behrendt C., Walter E., Scheckhuber C.Q., Entian K.-D., Reichert A.S. Synthetic Quantitative Array technology identifies the Ubp3-Bre5 deubiquitinase complex as a negative regulator of mitophagy. Cell Rep. 2015, 10. (Published online February 19, 2015). 10.1016/j.celrep.2015.2001.2044.
    • (2015) Cell Rep. , vol.10
    • Müller, M.1    Kötter, P.2    Behrendt, C.3    Walter, E.4    Scheckhuber, C.Q.5    Entian, K.-D.6    Reichert, A.S.7
  • 118
    • 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
  • 119
    • 79953163464 scopus 로고    scopus 로고
    • The Three Musketeers of Autophagy: phosphorylation, ubiquitylation and acetylation
    • McEwan D.G., Dikic I. The Three Musketeers of Autophagy: phosphorylation, ubiquitylation and acetylation. Trends Cell Biol. 2011, 21:195-201.
    • (2011) Trends Cell Biol. , vol.21 , pp. 195-201
    • McEwan, D.G.1    Dikic, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.