메뉴 건너뛰기




Volumn 95, Issue 1, 2015, Pages 14-25

Regulation of autophagy by protein post-translational modification

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE KINASE; BECLIN 1; CELL PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN P62; THIOL; UBIQUITIN; PROTEIN; THIOL DERIVATIVE;

EID: 84920080589     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.2014.131     Document Type: Review
Times cited : (132)

References (129)
  • 1
    • 2142663061 scopus 로고    scopus 로고
    • Ubiquitin as a central cellular regulator
    • Finley D, Ciechanover A, Varshavsky A. Ubiquitin as a central cellular regulator. Cell 2004;116:2.
    • (2004) Cell , vol.116 , pp. 2
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 2
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: Diversity, synthesis and function
    • Moremen KW, Tiemeyer M, Nairn AV. Vertebrate protein glycosylation: diversity, synthesis and function. Nat Rev Mol Cell Biol 2012;13:448-462.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 448-462
    • Moremen, K.W.1    Tiemeyer, M.2    Nairn, A.V.3
  • 3
    • 84859341928 scopus 로고    scopus 로고
    • Targeting protein lipidation in disease
    • Resh MD. Targeting protein lipidation in disease. Trends Mol Med 2012;18:206-214.
    • (2012) Trends Mol Med , vol.18 , pp. 206-214
    • Resh, M.D.1
  • 4
    • 84857895434 scopus 로고    scopus 로고
    • Protein kinases and phosphatases in the control of cell fate
    • Bononi A, Agnoletto C, De ME, et al. Protein kinases and phosphatases in the control of cell fate. Enzyme Res 2011;2011:329098.
    • (2011) Enzyme Res , vol.2011 , pp. 329098
    • Bononi, A.1    Agnoletto, C.2    De, M.E.3
  • 5
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for selfeating
    • Yorimitsu T, Klionsky DJ. Autophagy: molecular machinery for selfeating. Cell Death Differ 2005;12(Suppl 2):1542-1552.
    • (2005) Cell Death Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 6
    • 84879047011 scopus 로고    scopus 로고
    • Cellular metabolic and autophagic pathways: Traffic control by redox signaling
    • Dodson M, Darley-Usmar V, Zhang J. Cellular metabolic and autophagic pathways: traffic control by redox signaling. Free Radic Biol Med 2013;63:207-221.
    • (2013) Free Radic Biol Med , vol.63 , pp. 207-221
    • Dodson, M.1    Darley-Usmar, V.2    Zhang, J.3
  • 7
    • 84865592978 scopus 로고    scopus 로고
    • Amino acids and mTORC1: From lysosomes to disease
    • Efeyan A, Zoncu R, Sabatini DM. Amino acids and mTORC1: from lysosomes to disease. Trends Mol Med 2012;18:524-533.
    • (2012) Trends Mol Med , vol.18 , pp. 524-533
    • Efeyan, A.1    Zoncu, R.2    Sabatini, D.M.3
  • 8
    • 84884819157 scopus 로고    scopus 로고
    • Autophagosome formation-The role of ULK1 and Beclin1-PI3KC3 complexes in setting the stage
    • Wirth M, Joachim J, Tooze SA. Autophagosome formation-the role of ULK1 and Beclin1-PI3KC3 complexes in setting the stage. Semin Cancer Biol 2013;23:301-309.
    • (2013) Semin Cancer Biol , vol.23 , pp. 301-309
    • Wirth, M.1    Joachim, J.2    Tooze, S.A.3
  • 9
    • 42949139481 scopus 로고    scopus 로고
    • AMPK phosphorylation of raptor mediates a metabolic checkpoint
    • Gwinn DM, Shackelford DB, Egan DF, et al. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol Cell 2008;30: 214-226.
    • (2008) Mol Cell , vol.30 , pp. 214-226
    • Gwinn, D.M.1    Shackelford, D.B.2    Egan, D.F.3
  • 10
    • 79251587803 scopus 로고    scopus 로고
    • Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy
    • Egan DF, Shackelford DB, Mihaylova MM, et al. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. Science 2011;331:456-461.
    • (2011) Science , vol.331 , pp. 456-461
    • Egan, D.F.1    Shackelford, D.B.2    Mihaylova, M.M.3
  • 11
    • 79954576039 scopus 로고    scopus 로고
    • ULK1, mammalian target of rapamycin, and mitochondria: Linking nutrient availability and autophagy
    • Kundu M. ULK1, mammalian target of rapamycin, and mitochondria: linking nutrient availability and autophagy. Antioxid Redox Signal 2011;14:1953-1958.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1953-1958
    • Kundu, M.1
  • 12
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC. The phosphoinositide 3-kinase pathway. Science 2002; 296:1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 13
    • 33847397874 scopus 로고    scopus 로고
    • Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40
    • Vander HE, Lee SI, Bandhakavi S, et al. Insulin signalling to mTOR mediated by the Akt/PKB substrate PRAS40. Nat Cell Biol 2007;9: 316-323.
    • (2007) Nat Cell Biol , vol.9 , pp. 316-323
    • Vander, H.E.1    Lee, S.I.2    Bandhakavi, S.3
  • 14
    • 33947264077 scopus 로고    scopus 로고
    • PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase
    • Sancak Y, Thoreen CC, Peterson TR, et al. PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase. Mol Cell 2007;25:903-915.
    • (2007) Mol Cell , vol.25 , pp. 903-915
    • Sancak, Y.1    Thoreen, C.C.2    Peterson, T.R.3
  • 15
    • 0031026639 scopus 로고    scopus 로고
    • Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150. Ptdins 3-kinase complex
    • Panaretou C, Domin J, Cockcroft S, et al. Characterization of p150, an adaptor protein for the human phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150. Ptdins 3-kinase complex. J Biol Chem 1997;272: 2477-2485.
    • (1997) J Biol Chem , vol.272 , pp. 2477-2485
    • Panaretou, C.1    Domin, J.2    Cockcroft, S.3
  • 16
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • Itakura E, Mizushima N. Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy 2010;6:764-776.
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 17
    • 4944247868 scopus 로고    scopus 로고
    • Alfy, a novel FYVE domain-containing protein associated with protein granules and autophagic membranes
    • Simonsen A, Birkeland HC, Gillooly DJ, et al. Alfy, a novel FYVE domain-containing protein associated with protein granules and autophagic membranes. J Cell Sci 2004;117:4239-4251.
    • (2004) J Cell Sci , vol.117 , pp. 4239-4251
    • Simonsen, A.1    Birkeland, H.C.2    Gillooly, D.J.3
  • 18
    • 79952628267 scopus 로고    scopus 로고
    • The Beclin 1 network regulates autophagy and apoptosis
    • Kang R, Zeh HJ, Lotze MT, et al. The Beclin 1 network regulates autophagy and apoptosis. Cell Death Differ 2011;18:571-580.
    • (2011) Cell Death Differ , vol.18 , pp. 571-580
    • Kang, R.1    Zeh, H.J.2    Lotze, M.T.3
  • 19
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • Wei Y, Pattingre S, Sinha S, et al. JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol Cell 2008;30: 678-688.
    • (2008) Mol Cell , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3
  • 20
    • 67650270918 scopus 로고    scopus 로고
    • Phosphorylation of beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL
    • Zalckvar E, Berissi H, Eisenstein M, et al. Phosphorylation of Beclin 1 by DAP-kinase promotes autophagy by weakening its interactions with Bcl-2 and Bcl-XL. Autophagy 2009;5:720-722.
    • (2009) Autophagy , vol.5 , pp. 720-722
    • Zalckvar, E.1    Berissi, H.2    Eisenstein, M.3
  • 21
    • 84869147050 scopus 로고    scopus 로고
    • Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation
    • Wang RC, Wei Y, An Z, et al. Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation. Science 2012;338:956-959.
    • (2012) Science , vol.338 , pp. 956-959
    • Wang, R.C.1    Wei, Y.2    An, Z.3
  • 22
    • 84887581571 scopus 로고    scopus 로고
    • TRAPPIII is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy
    • Shirahama-Noda K, Kira S, Yoshimori T, et al. TRAPPIII is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy. J Cell Sci 2013;126:4963-4973.
    • (2013) J Cell Sci , vol.126 , pp. 4963-4973
    • Shirahama-Noda, K.1    Kira, S.2    Yoshimori, T.3
  • 23
    • 59449097721 scopus 로고    scopus 로고
    • Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy
    • He C, Baba M, Cao Y, et al. Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy. Mol Biol Cell 2008;19:5506-5516.
    • (2008) Mol Biol Cell , vol.19 , pp. 5506-5516
    • He, C.1    Baba, M.2    Cao, Y.3
  • 24
    • 33750366092 scopus 로고    scopus 로고
    • Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
    • Young AR, Chan EY, Hu XW, et al. Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci 2006;119:3888-3900.
    • (2006) J Cell Sci , vol.119 , pp. 3888-3900
    • Young, A.R.1    Chan, E.Y.2    Hu, X.W.3
  • 25
    • 84893742616 scopus 로고    scopus 로고
    • Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase
    • Papinski D, Schuschnig M, Reiter W, et al. Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase. Mol Cell 2014;53:471-483.
    • (2014) Mol Cell , vol.53 , pp. 471-483
    • Papinski, D.1    Schuschnig, M.2    Reiter, W.3
  • 26
    • 0034727876 scopus 로고    scopus 로고
    • Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: Possible role of vesicular transport in axonal elongation
    • Okazaki N, Yan J, Yuasa S, et al. Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation. Brain Res Mol Brain Res 2000;85:1-12.
    • (2000) Brain Res Mol Brain Res , vol.85 , pp. 1-12
    • Okazaki, N.1    Yan, J.2    Yuasa, S.3
  • 27
    • 77955875002 scopus 로고    scopus 로고
    • Regulation of the autophagy protein LC3 by phosphorylation
    • Cherra III SJ, Kulich SM, Uechi G, et al. Regulation of the autophagy protein LC3 by phosphorylation. J Cell Biol 2010;190:533-539.
    • (2010) J Cell Biol , vol.190 , pp. 533-539
    • Cherra, S.J.1    Kulich, S.M.2    Uechi, G.3
  • 28
    • 77952111333 scopus 로고    scopus 로고
    • Protein kinase C inhibits autophagy and phosphorylates LC3
    • Jiang H, Cheng D, Liu W, et al. Protein kinase C inhibits autophagy and phosphorylates LC3. Biochem Biophys Res Commun 2010;395: 471-476.
    • (2010) Biochem Biophys Res Commun , vol.395 , pp. 471-476
    • Jiang, H.1    Cheng, D.2    Liu, W.3
  • 29
    • 84870938108 scopus 로고    scopus 로고
    • MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins 1
    • Colecchia D, Strambi A, Sanzone S, et al. MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins 1. Autophagy 2012;8:1724-1740.
    • (2012) Autophagy , vol.8 , pp. 1724-1740
    • Colecchia, D.1    Strambi, A.2    Sanzone, S.3
  • 30
    • 84869222326 scopus 로고    scopus 로고
    • ATG8 family proteins act as scaffolds for assembly of the ULK complex: Sequence requirements for LC3-interacting region (LIR) motifs
    • Alemu EA, Lamark T, Torgersen KM, et al. ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs. J Biol Chem 2012;287: 39275-39290.
    • (2012) J Biol Chem , vol.287 , pp. 39275-39290
    • Alemu, E.A.1    Lamark, T.2    Torgersen, K.M.3
  • 31
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • Matsumoto G, Wada K, Okuno M, et al. Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. Mol Cell 2011;44:279-289.
    • (2011) Mol Cell , vol.44 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3
  • 32
    • 84881091197 scopus 로고    scopus 로고
    • Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation 2
    • Mao K, Chew LH, Inoue-Aono Y, et al. Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation 2. Proc Natl Acad Sci USA 2013;110:E2875-E2884.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E2875-E2884
    • Mao, K.1    Chew, L.H.2    Inoue-Aono, Y.3
  • 33
    • 70349739560 scopus 로고    scopus 로고
    • Characterization of the Atg17-Atg29-Atg31 complex specifically required for starvation-induced autophagy in Saccharomyces cerevisiae
    • Kabeya Y, Noda NN, Fujioka Y, et al. Characterization of the Atg17-Atg29-Atg31 complex specifically required for starvation-induced autophagy in Saccharomyces cerevisiae. Biochem Biophys Res Commun 2009;389:612-615.
    • (2009) Biochem Biophys Res Commun , vol.389 , pp. 612-615
    • Kabeya, Y.1    Noda, N.N.2    Fujioka, Y.3
  • 34
    • 84869388804 scopus 로고    scopus 로고
    • Integration of cellular bioenergetics with mitochondrial quality control and autophagy
    • Hill BG, Benavides GA, Lancaster Jr. JR, et al. Integration of cellular bioenergetics with mitochondrial quality control and autophagy. Biol Chem 2012;393:1485-1512.
    • (2012) Biol Chem , vol.393 , pp. 1485-1512
    • Hill, B.G.1    Benavides, G.A.2    Lancaster, J.R.3
  • 35
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda N, Sato S, Shiba K, et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J Cell Biol 2010;189:211-221.
    • (2010) J Cell Biol , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3
  • 36
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • Chen Y, Dorn GW. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science 2013;340:471-475.
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 37
    • 75949130828 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
    • Geisler S, Holmstrom KM, Skujat D, et al. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat Cell Biol 2010;12:119-131.
    • (2010) Nat Cell Biol , vol.12 , pp. 119-131
    • Geisler, S.1    Holmstrom, K.M.2    Skujat, D.3
  • 38
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg ME, Cooper JM, Chau KY, et al. 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
  • 39
    • 84857850213 scopus 로고    scopus 로고
    • Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy
    • Itakura E, Kishi-Itakura C, Koyama-Honda I, et al. Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy. J Cell Sci 2012;125:1488-1499.
    • (2012) J Cell Sci , vol.125 , pp. 1488-1499
    • Itakura, E.1    Kishi-Itakura, C.2    Koyama-Honda, I.3
  • 40
    • 84899789746 scopus 로고    scopus 로고
    • ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy
    • Wu W, Tian W, Hu Z, et al. ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy. EMBO Rep 2014;15: 566-575.
    • (2014) EMBO Rep , vol.15 , pp. 566-575
    • Wu, W.1    Tian, W.2    Hu, Z.3
  • 41
    • 80955177196 scopus 로고    scopus 로고
    • TFEB links autophagy to lysosomal biogenesis
    • Settembre C, Di MC, Polito VA, et al. TFEB links autophagy to lysosomal biogenesis. Science 2011;332:1429-1433.
    • (2011) Science , vol.332 , pp. 1429-1433
    • Settembre, C.1    Di, M.C.2    Polito, V.A.3
  • 42
    • 84857997408 scopus 로고    scopus 로고
    • A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
    • Settembre C, Zoncu R, Medina DL, et al. A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB. EMBO J 2012;31:1095-1108.
    • (2012) EMBO J , vol.31 , pp. 1095-1108
    • Settembre, C.1    Zoncu, R.2    Medina, D.L.3
  • 43
    • 84864874958 scopus 로고    scopus 로고
    • MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
    • Martina JA, Chen Y, Gucek M, et al. MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 2012;8:903-914.
    • (2012) Autophagy , vol.8 , pp. 903-914
    • Martina, J.A.1    Chen, Y.2    Gucek, M.3
  • 44
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han I, Kudlow JE. Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol Cell Biol 1997;17: 2550-2558.
    • (1997) Mol Cell Biol , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 45
    • 2342539803 scopus 로고    scopus 로고
    • O-GlcNAc modification: A nutritional sensor that modulates proteasome function
    • Zachara NE, Hart GW. O-GlcNAc modification: a nutritional sensor that modulates proteasome function. Trends Cell Biol 2004;14: 218-221.
    • (2004) Trends Cell Biol , vol.14 , pp. 218-221
    • Zachara, N.E.1    Hart, G.W.2
  • 46
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: The role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara NE, Hart GW. O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress. Biochim Biophys Acta 2004;1673: 13-28.
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 47
    • 30044438532 scopus 로고    scopus 로고
    • O-GlcNAc cycling: How a single sugar post-translational modification is changing the way we think about signaling networks
    • Slawson C, Housley MP, Hart GW. O-GlcNAc cycling: how a single sugar post-translational modification is changing the way we think about signaling networks. J Cell Biochem 2006;97:71-83.
    • (2006) J Cell Biochem , vol.97 , pp. 71-83
    • Slawson, C.1    Housley, M.P.2    Hart, G.W.3
  • 48
    • 84857627624 scopus 로고    scopus 로고
    • Protein O-linked beta-Nacetylglucosamine: A novel effector of cardiomyocyte metabolism and function
    • Darley-Usmar VM, Ball LE, Chatham JC. Protein O-linked beta-Nacetylglucosamine: a novel effector of cardiomyocyte metabolism and function. J Mol Cell Cardiol 2012;52:538-549.
    • (2012) J Mol Cell Cardiol , vol.52 , pp. 538-549
    • Darley-Usmar, V.M.1    Ball, L.E.2    Chatham, J.C.3
  • 49
    • 33644874204 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: Deciphering the "O-GlcNAc code"
    • Love DC, Hanover JA. The hexosamine signaling pathway: deciphering the "O-GlcNAc code". Sci STKE 2005;2005:re13.
    • (2005) Sci STKE , vol.2005 , pp. re13
    • Love, D.C.1    Hanover, J.A.2
  • 50
    • 2442687675 scopus 로고    scopus 로고
    • 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine
    • Guinez C, Lemoine J, Michalski JC, et al. 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine. Biochem Biophys Res Commun 2004;319:21-26.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 21-26
    • Guinez, C.1    Lemoine, J.2    Michalski, J.C.3
  • 51
    • 0032734974 scopus 로고    scopus 로고
    • O-GlcNAc and the control of gene expression
    • Comer FI, Hart GW. O-GlcNAc and the control of gene expression. Biochim Biophys Acta 1999;1473:161-171.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 161-171
    • Comer, F.I.1    Hart, G.W.2
  • 52
    • 2542446200 scopus 로고    scopus 로고
    • Accumulation of protein O-GlcNAc modification inhibits proteasomes in the brain and coincides with neuronal apoptosis in brain areas with high O-GlcNAc metabolism
    • Liu K, Paterson AJ, Zhang F, et al. Accumulation of protein O-GlcNAc modification inhibits proteasomes in the brain and coincides with neuronal apoptosis in brain areas with high O-GlcNAc metabolism. J Neurochem 2004;89:1044-1055.
    • (2004) J Neurochem , vol.89 , pp. 1044-1055
    • Liu, K.1    Paterson, A.J.2    Zhang, F.3
  • 53
  • 54
    • 52949123249 scopus 로고    scopus 로고
    • Cross-talk between GlcNAcylation and phosphorylation: Site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
    • Wang Z, Gucek M, Hart GW. Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc Natl Acad Sci USA 2008;105:13793-13798.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13793-13798
    • Wang, Z.1    Gucek, M.2    Hart, G.W.3
  • 55
    • 0034705030 scopus 로고    scopus 로고
    • The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny
    • Shafi R, Iyer SP, Ellies LG, et al. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny. Proc Natl Acad Sci USA 2000;97:5735-5739.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5735-5739
    • Shafi, R.1    Iyer, S.P.2    Ellies, L.G.3
  • 56
    • 84860872762 scopus 로고    scopus 로고
    • O-GlcNAcase is essential for embryonic development and maintenance of genomic stability
    • Yang YR, Song M, Lee H, et al. O-GlcNAcase is essential for embryonic development and maintenance of genomic stability. Aging Cell 2012;11:439-448.
    • (2012) Aging Cell , vol.11 , pp. 439-448
    • Yang, Y.R.1    Song, M.2    Lee, H.3
  • 57
    • 84867908726 scopus 로고    scopus 로고
    • O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases
    • Wang P, Lazarus BD, Forsythe ME, et al. O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases. Proc Natl Acad Sci USA 2012;109:17669-17674.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 17669-17674
    • Wang, P.1    Lazarus, B.D.2    Forsythe, M.E.3
  • 58
    • 84875210462 scopus 로고    scopus 로고
    • Cardiac O-GlcNAcylation blunts autophagic signaling in the diabetic heart
    • Marsh SA, Powell PC, Dell'italia LJ, et al. Cardiac O-GlcNAcylation blunts autophagic signaling in the diabetic heart. Life Sci 2013;92: 648-656.
    • (2013) Life Sci , vol.92 , pp. 648-656
    • Marsh, S.A.1    Powell, P.C.2    Dell'italia, L.J.3
  • 59
    • 84898613353 scopus 로고    scopus 로고
    • Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)
    • Bullen JW, Balsbaugh JL, Chanda D, et al. Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK). J Biol Chem 2014;289: 10592-10606.
    • (2014) J Biol Chem , vol.289 , pp. 10592-10606
    • Bullen, J.W.1    Balsbaugh, J.L.2    Chanda, D.3
  • 60
    • 84861306218 scopus 로고    scopus 로고
    • Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling
    • Wang S, Huang X, Sun D, et al. Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling. PLoS ONE 2012;7:e37427.
    • (2012) PLoS ONE , vol.7 , pp. e37427
    • Wang, S.1    Huang, X.2    Sun, D.3
  • 61
    • 0344642959 scopus 로고    scopus 로고
    • Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex
    • Akimoto Y, Comer FI, Cole RN, et al. Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex. Brain Res 2003;966:194-205.
    • (2003) Brain Res , vol.966 , pp. 194-205
    • Akimoto, Y.1    Comer, F.I.2    Cole, R.N.3
  • 62
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: Cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
    • Gao Y, Wells L, Comer FI, et al. Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain. J Biol Chem 2001;276:9838-9845.
    • (2001) J Biol Chem , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3
  • 63
    • 43249097865 scopus 로고    scopus 로고
    • Aging leads to increased levels of protein O-linked N-acetylglucosamine in heart, aorta, brain and skeletal muscle in Brown-Norway rats
    • Fulop N, Feng W, Xing D, et al. Aging leads to increased levels of protein O-linked N-acetylglucosamine in heart, aorta, brain and skeletal muscle in Brown-Norway rats. Biogerontology 2008;9:139-151.
    • (2008) Biogerontology , vol.9 , pp. 139-151
    • Fulop, N.1    Feng, W.2    Xing, D.3
  • 64
    • 84865191053 scopus 로고    scopus 로고
    • Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain
    • Liu Y, Li X, Yu Y, et al. Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain. PLoS ONE 2012;7:e43724.
    • (2012) PLoS ONE , vol.7 , pp. e43724
    • Liu, Y.1    Li, X.2    Yu, Y.3
  • 65
    • 16644369554 scopus 로고    scopus 로고
    • The potential role of tau protein O-glycosylation in Alzheimer's disease
    • Robertson LA, Moya KL, Breen KC. The potential role of tau protein O-glycosylation in Alzheimer's disease. J Alzheimers. Dis 2004;6: 489-495.
    • (2004) J Alzheimers. Dis , vol.6 , pp. 489-495
    • Robertson, L.A.1    Moya, K.L.2    Breen, K.C.3
  • 66
    • 67650072530 scopus 로고    scopus 로고
    • Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease
    • Liu F, Shi J, Tanimukai H, et al. Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease. Brain 2009;132:1820-1832.
    • (2009) Brain , vol.132 , pp. 1820-1832
    • Liu, F.1    Shi, J.2    Tanimukai, H.3
  • 67
    • 84858664547 scopus 로고    scopus 로고
    • Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation
    • Yuzwa SA, Shan X, Macauley MS, et al. Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation. Nat Chem Biol 2012;8:393-399.
    • (2012) Nat Chem Biol , vol.8 , pp. 393-399
    • Yuzwa, S.A.1    Shan, X.2    MacAuley, M.S.3
  • 68
    • 47649114560 scopus 로고    scopus 로고
    • A potent mechanisminspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo
    • Yuzwa SA, Macauley MS, Heinonen JE, et al. A potent mechanisminspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat Chem Biol 2008;4:483-490.
    • (2008) Nat Chem Biol , vol.4 , pp. 483-490
    • Yuzwa, S.A.1    MacAuley, M.S.2    Heinonen, J.E.3
  • 69
    • 84859819548 scopus 로고    scopus 로고
    • Differential effects of an O-GlcNAcase inhibitor on tau phosphorylation
    • Yu Y, Zhang L, Li X, et al. Differential effects of an O-GlcNAcase inhibitor on tau phosphorylation. PLoS ONE 2012;7:e35277.
    • (2012) PLoS ONE , vol.7 , pp. e35277
    • Yu, Y.1    Zhang, L.2    Li, X.3
  • 70
    • 84871257892 scopus 로고    scopus 로고
    • O-GlcNAc modification prevents peptide-dependent acceleration of alpha-synuclein aggregation
    • Marotta NP, Cherwien CA, Abeywardana T, et al. O-GlcNAc modification prevents peptide-dependent acceleration of alpha-synuclein aggregation. Chembiochem 2012;13:2665-2670.
    • (2012) Chembiochem , vol.13 , pp. 2665-2670
    • Marotta, N.P.1    Cherwien, C.A.2    Abeywardana, T.3
  • 71
    • 84900424968 scopus 로고    scopus 로고
    • Decreased O-linked GlcNAcylation protects from cytotoxicity mediated by huntingtin exon1 protein fragment
    • Kumar A, Singh PK, Parihar R, et al. Decreased O-linked GlcNAcylation protects from cytotoxicity mediated by huntingtin exon1 protein fragment. J Biol Chem 2014;289:13543-13553.
    • (2014) J Biol Chem , vol.289 , pp. 13543-13553
    • Kumar, A.1    Singh, P.K.2    Parihar, R.3
  • 72
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • Hanada T, Noda NN, Satomi Y, et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 2007;282:37298-37302.
    • (2007) J Biol Chem , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3
  • 73
    • 81855167585 scopus 로고    scopus 로고
    • DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(betaTrCP) E3 ubiquitin ligase and regulates survival and autophagy
    • Zhao Y, Xiong X, Sun Y. DEPTOR, an mTOR inhibitor, is a physiological substrate of SCF(betaTrCP) E3 ubiquitin ligase and regulates survival and autophagy. Mol Cell 2011;44:304-316.
    • (2011) Mol Cell , vol.44 , pp. 304-316
    • Zhao, Y.1    Xiong, X.2    Sun, Y.3
  • 74
    • 81855181738 scopus 로고    scopus 로고
    • MTOR drives its own activation via SCF(betaTrCP)-dependent degradation of the mTOR inhibitor DEPTOR
    • Gao D, Inuzuka H, Tan MK, et al. mTOR drives its own activation via SCF(betaTrCP)-dependent degradation of the mTOR inhibitor DEPTOR. Mol Cell 2011;44:290-303.
    • (2011) Mol Cell , vol.44 , pp. 290-303
    • Gao, D.1    Inuzuka, H.2    Tan, M.K.3
  • 75
    • 84868148976 scopus 로고    scopus 로고
    • Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection
    • Kuang E, Okumura CY, Sheffy-Levin S, et al. Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection. PLoS Genet 2012;8:e1003007.
    • (2012) PLoS Genet , vol.8 , pp. e1003007
    • Kuang, E.1    Okumura, C.Y.2    Sheffy-Levin, S.3
  • 76
    • 84876488191 scopus 로고    scopus 로고
    • MTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6
    • Nazio F, Strappazzon F, Antonioli M, et al. mTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6. Nat Cell Biol 2013;15:406-416.
    • (2013) Nat Cell Biol , vol.15 , pp. 406-416
    • Nazio, F.1    Strappazzon, F.2    Antonioli, M.3
  • 77
    • 77953858790 scopus 로고    scopus 로고
    • TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy
    • Shi CS, Kehrl JH. TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy. Sci Signal 2010;3:ra42.
    • (2010) Sci Signal , vol.3 , pp. ra42
    • Shi, C.S.1    Kehrl, J.H.2
  • 78
    • 78649653044 scopus 로고    scopus 로고
    • Parkin mono-ubiquitinates Bcl-2 and regulates autophagy
    • Chen D, Gao F, Li B, et al. Parkin mono-ubiquitinates Bcl-2 and regulates autophagy. J Biol Chem 2010;285:38214-38223.
    • (2010) J Biol Chem , vol.285 , pp. 38214-38223
    • Chen, D.1    Gao, F.2    Li, B.3
  • 79
    • 84055219407 scopus 로고    scopus 로고
    • Nedd4-dependent lysine-11-linked polyubiquitination of the tumour suppressor Beclin 1
    • Platta HW, Abrahamsen H, Thoresen SB, et al. Nedd4-dependent lysine-11-linked polyubiquitination of the tumour suppressor Beclin 1. Biochem J 2012;441:399-406.
    • (2012) Biochem J , vol.441 , pp. 399-406
    • Platta, H.W.1    Abrahamsen, H.2    Thoresen, S.B.3
  • 80
    • 80052564638 scopus 로고    scopus 로고
    • RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1
    • Tang F, Wang B, Li N, et al. RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1. PLoS ONE 2011;6:e24367.
    • (2011) PLoS ONE , vol.6 , pp. e24367
    • Tang, F.1    Wang, B.2    Li, N.3
  • 81
    • 84874610790 scopus 로고    scopus 로고
    • UBR box N-recognin-4 (UBR4), an N-recognin of the N-end rule pathway, and its role in yolk sac vascular development and autophagy
    • Tasaki T, Kim ST, Zakrzewska A, et al. UBR box N-recognin-4 (UBR4), an N-recognin of the N-end rule pathway, and its role in yolk sac vascular development and autophagy. Proc Natl Acad Sci USA 2013;110:3800-3805.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 3800-3805
    • Tasaki, T.1    Kim, S.T.2    Zakrzewska, A.3
  • 82
    • 84896265496 scopus 로고    scopus 로고
    • Ubiquitylation by the Ltn1 E3 ligase protects 60S ribosomes from starvation-induced selective autophagy
    • Ossareh-Nazari B, Nino CA, Bengtson MH, et al. Ubiquitylation by the Ltn1 E3 ligase protects 60S ribosomes from starvation-induced selective autophagy. J Cell Biol 2014;204:909-917.
    • (2014) J Cell Biol , vol.204 , pp. 909-917
    • Ossareh-Nazari, B.1    Nino, C.A.2    Bengtson, M.H.3
  • 83
    • 84861204926 scopus 로고    scopus 로고
    • PINK1- and Parkin-mediated mitophagy at a glance
    • Jin SM, Youle RJ. PINK1- and Parkin-mediated mitophagy at a glance. J Cell Sci 2012;125:795-799.
    • (2012) J Cell Sci , vol.125 , pp. 795-799
    • Jin, S.M.1    Youle, R.J.2
  • 84
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
    • Tanaka A, Cleland MM, Xu S, et al. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J Cell Biol 2010;191:1367-1380.
    • (2010) J Cell Biol , vol.191 , pp. 1367-1380
    • Tanaka, A.1    Cleland, M.M.2    Xu, S.3
  • 85
    • 78649300971 scopus 로고    scopus 로고
    • P62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra D, Kane LA, Hauser DN, et al. p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 2010;6:1090-1106.
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3
  • 86
    • 84870013071 scopus 로고    scopus 로고
    • Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy
    • Sun Y, Vashisht AA, Tchieu J, et al. Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy. J Biol Chem 2012;287:40652-40660.
    • (2012) J Biol Chem , vol.287 , pp. 40652-40660
    • Sun, Y.1    Vashisht, A.A.2    Tchieu, J.3
  • 87
    • 60449108890 scopus 로고    scopus 로고
    • Miro1 is a calcium sensor for glutamate receptor-dependent localization of mitochondria at synapses
    • Macaskill AF, Rinholm JE, Twelvetrees AE, et al. Miro1 is a calcium sensor for glutamate receptor-dependent localization of mitochondria at synapses. Neuron 2009;61:541-555.
    • (2009) Neuron , vol.61 , pp. 541-555
    • MacAskill, A.F.1    Rinholm, J.E.2    Twelvetrees, A.E.3
  • 88
    • 65649107618 scopus 로고    scopus 로고
    • Drosophila Miro is required for both anterograde and retrograde axonal mitochondrial transport
    • Russo GJ, Louie K, Wellington A, et al. Drosophila Miro is required for both anterograde and retrograde axonal mitochondrial transport. J Neurosci 2009;29:5443-5455.
    • (2009) J Neurosci , vol.29 , pp. 5443-5455
    • Russo, G.J.1    Louie, K.2    Wellington, A.3
  • 89
    • 79954520907 scopus 로고    scopus 로고
    • Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy
    • Chan NC, Salazar AM, Pham AH, et al. Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy. Hum Mol Genet 2011;20:1726-1737.
    • (2011) Hum Mol Genet , vol.20 , pp. 1726-1737
    • Chan, N.C.1    Salazar, A.M.2    Pham, A.H.3
  • 90
    • 81055140895 scopus 로고    scopus 로고
    • PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility
    • Wang X, Winter D, Ashrafi G, et al. PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 2011;147:893-906.
    • (2011) Cell , vol.147 , pp. 893-906
    • Wang, X.1    Winter, D.2    Ashrafi, G.3
  • 91
    • 84901407276 scopus 로고    scopus 로고
    • K27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase
    • Birsa N, Norkett R, Wauer T, et al. K27 ubiquitination of the mitochondrial transport protein Miro is dependent on serine 65 of the Parkin ubiquitin ligase. J Biol Chem 2014;289:14569-14582.
    • (2014) J Biol Chem , vol.289 , pp. 14569-14582
    • Birsa, N.1    Norkett, R.2    Wauer, T.3
  • 92
    • 84890339047 scopus 로고    scopus 로고
    • Hexokinase activity is required for recruitment of parkin to depolarized mitochondria
    • McCoy MK, Kaganovich A, Rudenko IN, et al. Hexokinase activity is required for recruitment of parkin to depolarized mitochondria. Hum Mol Genet 2014;23:145-156.
    • (2014) Hum Mol Genet , vol.23 , pp. 145-156
    • McCoy, M.K.1    Kaganovich, A.2    Rudenko, I.N.3
  • 93
    • 84868384387 scopus 로고    scopus 로고
    • Mitochondrial hexokinase HKI is a novel substrate of the Parkin ubiquitin ligase
    • Okatsu K, Iemura S, Koyano F, et al. Mitochondrial hexokinase HKI is a novel substrate of the Parkin ubiquitin ligase. Biochem Biophys Res Commun 2012;428:197-202.
    • (2012) Biochem Biophys Res Commun , vol.428 , pp. 197-202
    • Okatsu, K.1    Iemura, S.2    Koyano, F.3
  • 94
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • Sarraf SA, Raman M, Guarani-Pereira V, et al. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature 2013;496:372-376.
    • (2013) Nature , vol.496 , pp. 372-376
    • Sarraf, S.A.1    Raman, M.2    Guarani-Pereira, V.3
  • 95
    • 84903179483 scopus 로고    scopus 로고
    • The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
    • Bingol B, Tea JS, Phu L, et al. The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 2014;510: 370-375.
    • (2014) Nature , vol.510 , pp. 370-375
    • Bingol, B.1    Tea, J.S.2    Phu, L.3
  • 96
    • 84876524198 scopus 로고    scopus 로고
    • Regulation of mitophagy by the Gp78 E3 ubiquitin ligase
    • Fu M, St-Pierre P, Shankar J, et al. Regulation of mitophagy by the Gp78 E3 ubiquitin ligase. Mol Biol Cell 2013;24:1153-1162.
    • (2013) Mol Biol Cell , vol.24 , pp. 1153-1162
    • Fu, M.1    St-Pierre, P.2    Shankar, J.3
  • 97
    • 33749253910 scopus 로고    scopus 로고
    • MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology
    • Nakamura N, Kimura Y, Tokuda M, et al. MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep 2006;7:1019-1022.
    • (2006) EMBO Rep , vol.7 , pp. 1019-1022
    • Nakamura, N.1    Kimura, Y.2    Tokuda, M.3
  • 98
    • 76649142385 scopus 로고    scopus 로고
    • Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynaminrelated protein 1 and mitofusin 1
    • Park YY, Lee S, Karbowski M, et al. Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynaminrelated protein 1 and mitofusin 1. J Cell Sci 2010;123:619-626.
    • (2010) J Cell Sci , vol.123 , pp. 619-626
    • Park, Y.Y.1    Lee, S.2    Karbowski, M.3
  • 99
    • 84883187967 scopus 로고    scopus 로고
    • Emerging roles of E3 ubiquitin ligases in autophagy
    • Kuang E, Qi J, Ronai Z. Emerging roles of E3 ubiquitin ligases in autophagy. Trends Biochem Sci 2013;38:453-460.
    • (2013) Trends Biochem Sci , vol.38 , pp. 453-460
    • Kuang, E.1    Qi, J.2    Ronai, Z.3
  • 100
    • 79953163464 scopus 로고    scopus 로고
    • The Three Musketeers of Autophagy: Phosphorylation, ubiquitylation and acetylation
    • McEwan DG, 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
  • 101
    • 84892859905 scopus 로고    scopus 로고
    • Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy
    • Rogov V, Dotsch V, Johansen T, et al. Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. Mol Cell 2014;53:167-178.
    • (2014) Mol Cell , vol.53 , pp. 167-178
    • Rogov, V.1    Dotsch, V.2    Johansen, T.3
  • 102
    • 84863609087 scopus 로고    scopus 로고
    • The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and promotes the sequestration and clearance of ubiquitinated proteins into the aggresome
    • Fusco C, Micale L, Egorov M, et al. The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and promotes the sequestration and clearance of ubiquitinated proteins into the aggresome. PLoS ONE 2012;7:e40440.
    • (2012) PLoS ONE , vol.7 , pp. e40440
    • Fusco, C.1    Micale, L.2    Egorov, M.3
  • 103
    • 77954599053 scopus 로고    scopus 로고
    • P62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • Jain A, Lamark T, Sjottem E, et al. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J Biol Chem 2010;285:22576-22591.
    • (2010) J Biol Chem , vol.285 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjottem, E.3
  • 104
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu M, Kurokawa H, Waguri S, et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat Cell Biol 2010;12:213-223.
    • (2010) Nat Cell Biol , vol.12 , pp. 213-223
    • Komatsu, M.1    Kurokawa, H.2    Waguri, S.3
  • 105
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S, Xiang F, Yakovenko A, et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 2005;308:1599-1603.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3
  • 106
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between Keap1 and p62
    • Lau A, Wang XJ, Zhao F, et al. A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62. Mol Cell Biol 2010;30:3275-3285.
    • (2010) Mol Cell Biol , vol.30 , pp. 3275-3285
    • Lau, A.1    Wang, X.J.2    Zhao, F.3
  • 107
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • Wild P, Farhan H, McEwan DG, et al. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 2011;333:228-233.
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1    Farhan, H.2    McEwan, D.G.3
  • 108
    • 37649017266 scopus 로고    scopus 로고
    • NIX is required for programmed mitochondrial clearance during reticulocyte maturation
    • Schweers RL, Zhang J, Randall MS, et al. NIX is required for programmed mitochondrial clearance during reticulocyte maturation. Proc Natl Acad Sci USA 2007;104:19500-19505.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19500-19505
    • Schweers, R.L.1    Zhang, J.2    Randall, M.S.3
  • 109
    • 47049100413 scopus 로고    scopus 로고
    • Essential role for Nix in autophagic maturation of erythroid cells
    • Sandoval H, Thiagarajan P, Dasgupta SK, et al. Essential role for Nix in autophagic maturation of erythroid cells. Nature 2008;454: 232-235.
    • (2008) Nature , vol.454 , pp. 232-235
    • Sandoval, H.1    Thiagarajan, P.2    Dasgupta, S.K.3
  • 110
    • 67549101188 scopus 로고    scopus 로고
    • Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
    • Zhang J, Ney PA. Role of BNIP3 and NIX in cell death, autophagy, and mitophagy. Cell Death Differ 2009;16:939-946.
    • (2009) Cell Death Differ , vol.16 , pp. 939-946
    • Zhang, J.1    Ney, P.A.2
  • 111
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
    • Liu L, Feng D, Chen G, et al. Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat Cell Biol 2012;14:177-185.
    • (2012) Nat Cell Biol , vol.14 , pp. 177-185
    • Liu, L.1    Feng, D.2    Chen, G.3
  • 112
    • 84895755121 scopus 로고    scopus 로고
    • Nucleocytosolic depletion of the energy metabolite acetyl-coenzyme a stimulates autophagy and prolongs lifespan
    • Eisenberg T, Schroeder S, Andryushkova A, et al. Nucleocytosolic depletion of the energy metabolite acetyl-coenzyme a stimulates autophagy and prolongs lifespan. Cell Metab 2014;19:431-444.
    • (2014) Cell Metab , vol.19 , pp. 431-444
    • Eisenberg, T.1    Schroeder, S.2    Andryushkova, A.3
  • 113
    • 84896713080 scopus 로고    scopus 로고
    • Regulation of autophagy by cytosolic acetyl-coenzyme A
    • Marino G, Pietrocola F, Eisenberg T, et al. Regulation of autophagy by cytosolic acetyl-coenzyme A. Mol Cell 2014;53:710-725.
    • (2014) Mol Cell , vol.53 , pp. 710-725
    • Marino, G.1    Pietrocola, F.2    Eisenberg, T.3
  • 114
    • 84882846112 scopus 로고    scopus 로고
    • The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy
    • Fullgrabe J, Lynch-Day MA, Heldring N, et al. The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy. Nature 2013;500:468-471.
    • (2013) Nature , vol.500 , pp. 468-471
    • Fullgrabe, J.1    Lynch-Day, M.A.2    Heldring, N.3
  • 115
    • 84899444482 scopus 로고    scopus 로고
    • Reactive oxygen species, AMP-activated protein kinase, and the transcription cofactor p300 regulate alpha-Tubulin Acetyltransferase-1 (alphaTAT-1/MEC-17)- dependent microtubule hyperacetylation during cell stress
    • Mackeh R, Lorin S, Ratier A, et al. Reactive oxygen species, AMP-activated protein kinase, and the transcription cofactor p300 regulate alpha-Tubulin Acetyltransferase-1 (alphaTAT-1/MEC-17)- dependent microtubule hyperacetylation during cell stress. J Biol Chem 2014;289:11816-11828.
    • (2014) J Biol Chem , vol.289 , pp. 11816-11828
    • MacKeh, R.1    Lorin, S.2    Ratier, A.3
  • 116
    • 65249106104 scopus 로고    scopus 로고
    • Regulation of autophagy by the p300 acetyltransferase
    • Lee IH, Finkel T. Regulation of autophagy by the p300 acetyltransferase. J Biol Chem 2009;284:6322-6328.
    • (2009) J Biol Chem , vol.284 , pp. 6322-6328
    • Lee, I.H.1    Finkel, T.2
  • 117
    • 84860172051 scopus 로고    scopus 로고
    • GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to autophagy
    • Lin SY, Li TY, Liu Q, et al. GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to autophagy. Science 2012;336:477-481.
    • (2012) Science , vol.336 , pp. 477-481
    • Lin, S.Y.1    Li, T.Y.2    Liu, Q.3
  • 118
    • 84888841680 scopus 로고    scopus 로고
    • LC3B-II deacetylation by histone deacetylase 6 is involved in serum-starvation-induced autophagic degradation
    • Liu KP, Zhou D, Ouyang DY, et al. LC3B-II deacetylation by histone deacetylase 6 is involved in serum-starvation-induced autophagic degradation. Biochem Biophys Res Commun 2013;441:970-975.
    • (2013) Biochem Biophys Res Commun , vol.441 , pp. 970-975
    • Liu, K.P.1    Zhou, D.2    Ouyang, D.Y.3
  • 119
    • 41549138483 scopus 로고    scopus 로고
    • A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
    • Lee IH, Cao L, Mostoslavsky R, et al. A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proc Natl Acad Sci USA 2008;105:3374-3379.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3374-3379
    • Lee, I.H.1    Cao, L.2    Mostoslavsky, R.3
  • 120
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong H, Then F, Melia Jr. TJ, et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 2009;137: 60-72.
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1    Then, F.2    Melia, T.J.3
  • 121
    • 84856729192 scopus 로고    scopus 로고
    • Mitochondrial thiols in antioxidant protection and redox signaling: Distinct roles for glutathionylation and other thiol modifications
    • Murphy MP. Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications. Antioxid Redox Signal 2012;16:476-495.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 476-495
    • Murphy, M.P.1
  • 122
    • 84856762901 scopus 로고    scopus 로고
    • Redox-based regulation of apoptosis: S-glutathionylation as a regulatory mechanism to control cell death
    • Anathy V, Roberson EC, Guala AS, et al. Redox-based regulation of apoptosis: S-glutathionylation as a regulatory mechanism to control cell death. Antioxid Redox Signal 2012;16:496-505.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 496-505
    • Anathy, V.1    Roberson, E.C.2    Guala, A.S.3
  • 123
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy, mitochondria and oxidative stress: Cross-talk and redox signalling
    • Lee J, Giordano S, Zhang J. Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling. Biochem J 2012;441:523-540.
    • (2012) Biochem J , vol.441 , pp. 523-540
    • Lee, J.1    Giordano, S.2    Zhang, J.3
  • 124
    • 84898785937 scopus 로고    scopus 로고
    • Redox regulation of antioxidants, autophagy, and the response to stress: Implications for electrophile therapeutics
    • Levonen AL, Hill BG, Kansanen E, et al. Redox regulation of antioxidants, autophagy, and the response to stress: Implications for electrophile therapeutics. Free Radic Biol Med 2014;71C:196-207.
    • (2014) Free Radic Biol Med , vol.71 C , pp. 196-207
    • Levonen, A.L.1    Hill, B.G.2    Kansanen, E.3
  • 125
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, et al. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 2007;26:1749-1760.
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3
  • 126
    • 33745280651 scopus 로고    scopus 로고
    • Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitinprotein ligase with monoubiquitylation capacity
    • Hampe C, Ardila-Osorio H, Fournier M, et al. Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitinprotein ligase with monoubiquitylation capacity. Hum Mol Genet 2006;15:2059-2075.
    • (2006) Hum Mol Genet , vol.15 , pp. 2059-2075
    • Hampe, C.1    Ardila-Osorio, H.2    Fournier, M.3
  • 127
    • 84875910694 scopus 로고    scopus 로고
    • Sulfhydration mediates neuroprotective actions of parkin
    • Vandiver MS, Paul BD, Xu R, et al. Sulfhydration mediates neuroprotective actions of parkin. Nat Commun 2013;4:1626.
    • (2013) Nat Commun , vol.4 , pp. 1626
    • Vandiver, M.S.1    Paul, B.D.2    Xu, R.3
  • 128
    • 77949623516 scopus 로고    scopus 로고
    • Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1
    • Krebiehl G, Ruckerbauer S, Burbulla LF, et al. Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1. PLoS ONE 2010;5:e9367.
    • (2010) PLoS ONE , vol.5 , pp. e9367
    • Krebiehl, G.1    Ruckerbauer, S.2    Burbulla, L.F.3
  • 129
    • 84892163616 scopus 로고    scopus 로고
    • Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease
    • Giordano S, Darley-Usmar V, Zhang J. Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease. Redox Biol 2014;2:82-90.
    • (2014) Redox Biol , vol.2 , pp. 82-90
    • Giordano, S.1    Darley-Usmar, V.2    Zhang, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.