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Volumn 12, Issue 11, 2016, Pages 2197-2212

The arginylation branch of the N-end rule pathway positively regulates cellular autophagic flux and clearance of proteotoxic proteins

Author keywords

ATE1; autophagy; HSPA5; N end rule pathway; neurodegenerative disease; para chloroamphetamine; ubiquitin proteasome system

Indexed keywords

AMINO ACID; ARGININE; CHLORAMPHETAMINE; DNA; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 5; HUNTINGTIN; UNCLASSIFIED DRUG; BIOLOGICAL MARKER; MOLECULAR CHAPERONE GRP78; MOLECULAR LIBRARY; PROTEASOME; PROTEIN; PROTEIN AGGREGATE; TAU PROTEIN;

EID: 84988310722     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.1080/15548627.2016.1222991     Document Type: Article
Times cited : (23)

References (68)
  • 1
    • 80054958053 scopus 로고    scopus 로고
    • The N-end rule pathway: emerging functions and molecular principles of substrate recognition
    • 22016057
    • S.M.Sriram, B.Y.Kim, Y.T.Kwon. The N-end rule pathway:emerging functions and molecular principles of substrate recognition. Nat Rev Mol Cell Biol 2011; 12:735-47; PMID:22016057; http://dx.doi.org/10.1038/nrm3217
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 735-747
    • Sriram, S.M.1    Kim, B.Y.2    Kwon, Y.T.3
  • 2
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • 21633985
    • A.Varshavsky. The N-end rule pathway and regulation by proteolysis. Protein Sci 2011; 20(8):1298-345; PMID:21633985; http://dx.doi.org/10.1002/pro.666
    • (2011) Protein Sci , vol.20 , Issue.8 , pp. 1298-1345
    • Varshavsky, A.1
  • 3
    • 77956162428 scopus 로고    scopus 로고
    • Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis
    • 20636328
    • F.A.Cerda-Maira, M.J.Pearce, M.Fuortes, W.R.Bishai, S.R.Hubbard, K.H.Darwin. Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis. Mol Microbiol 2010; 77:1123-35; PMID:20636328; http://dx.doi.org/10.1111/j.1365-2958.2010.07276.x
    • (2010) Mol Microbiol , vol.77 , pp. 1123-1135
    • Cerda-Maira, F.A.1    Pearce, M.J.2    Fuortes, M.3    Bishai, W.R.4    Hubbard, S.R.5    Darwin, K.H.6
  • 5
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: proteases in the machine age
    • 14990998
    • C.M.Pickart, R.E.Cohen. Proteasomes and their kin:proteases in the machine age. Nat Rev Mol Cell Biol 2004; 5:177-87; PMID:14990998; http://dx.doi.org/10.1038/nrm1336
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 6
    • 84861881296 scopus 로고    scopus 로고
    • The ubiquitin system, an immense realm
    • 22663079
    • A.Varshavsky. The ubiquitin system, an immense realm. Annu Rev Biochem 2012; 81:167-76; PMID:22663079; http://dx.doi.org/10.1146/annurev-biochem-051910-094049
    • (2012) Annu Rev Biochem , vol.81 , pp. 167-176
    • Varshavsky, A.1
  • 7
    • 84946223231 scopus 로고    scopus 로고
    • Pharmacological modulation of the N-End Rule Pathway and its Therapeutic Implications
    • 26434644
    • J.H.Lee, Y.Jiang, Y.T.Kwon, M.J.Lee. Pharmacological modulation of the N-End Rule Pathway and its Therapeutic Implications. Trends Pharmacol Sci 2015; 36(11):782-97; PMID:26434644; http://dx.doi.org/10.1016/j.tips.2015.07.004
    • (2015) Trends Pharmacol Sci , vol.36 , Issue.11 , pp. 782-797
    • Lee, J.H.1    Jiang, Y.2    Kwon, Y.T.3    Lee, M.J.4
  • 8
    • 77149120798 scopus 로고    scopus 로고
    • N-terminal acetylation of cellular proteins creates specific degradation signals
    • 20110468
    • C.S.Hwang, A.Shemorry, A.Varshavsky. N-terminal acetylation of cellular proteins creates specific degradation signals. Science 2010; 327:973-7; PMID:20110468; http://dx.doi.org/10.1126/science.1183147
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 9
    • 84878195272 scopus 로고    scopus 로고
    • Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway
    • 23603116
    • A.Shemorry, C.S.Hwang, A.Varshavsky. Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway. Mol Cell 2013; 50:540-51; PMID:23603116; http://dx.doi.org/10.1016/j.molcel.2013.03.018
    • (2013) Mol Cell , vol.50 , pp. 540-551
    • Shemorry, A.1    Hwang, C.S.2    Varshavsky, A.3
  • 10
    • 23344452833 scopus 로고    scopus 로고
    • A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons
    • 16055722
    • T.Tasaki, L.C.Mulder, A.Iwamatsu, M.J.Lee, I.V.Davydov, A.Varshavsky, M.Muesing, Y.T.Kwon. A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons. Mol Cell Biol 2005; 25:7120-36; PMID:16055722; http://dx.doi.org/10.1128/MCB.25.16.7120-7136.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 7120-7136
    • Tasaki, T.1    Mulder, L.C.2    Iwamatsu, A.3    Lee, M.J.4    Davydov, I.V.5    Varshavsky, A.6    Muesing, M.7    Kwon, Y.T.8
  • 11
    • 77957805791 scopus 로고    scopus 로고
    • Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases
    • 20835240
    • W.S.Choi, B.C.Jeong, Y.J.Joo, M.R.Lee, J.Kim, M.J.Eck, H.K.Song. Structural basis for the recognition of N-end rule substrates by the UBR box of ubiquitin ligases. Nat Struct Mol Biol 2010; 17:1175-81; PMID:20835240; http://dx.doi.org/10.1038/nsmb.1907
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1175-1181
    • Choi, W.S.1    Jeong, B.C.2    Joo, Y.J.3    Lee, M.R.4    Kim, J.5    Eck, M.J.6    Song, H.K.7
  • 12
    • 77957790301 scopus 로고    scopus 로고
    • Structural basis of substrate recognition and specificity in the N-end rule pathway
    • 20835242
    • E.Matta-Camacho, G.Kozlov, F.F.Li, K.Gehring. Structural basis of substrate recognition and specificity in the N-end rule pathway. Nat Struct Mol Biol 2010; 17:1182-7; PMID:20835242; http://dx.doi.org/10.1038/nsmb.1894
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1182-1187
    • Matta-Camacho, E.1    Kozlov, G.2    Li, F.F.3    Gehring, K.4
  • 13
    • 67049154051 scopus 로고    scopus 로고
    • Molecular basis of substrate selection by the N-end rule adaptor protein ClpS
    • 19451643
    • G.Roman-Hernandez, R.A.Grant, R.T.Sauer, T.A.Baker. Molecular basis of substrate selection by the N-end rule adaptor protein ClpS. Proc Natl Acad Sci U S A 2009; 106:8888-93; PMID:19451643; http://dx.doi.org/10.1073/pnas.0903614106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8888-8893
    • Roman-Hernandez, G.1    Grant, R.A.2    Sauer, R.T.3    Baker, T.A.4
  • 14
    • 84880010156 scopus 로고    scopus 로고
    • Characterization of mammalian N-degrons and development of heterovalent inhibitors of the N-end rule pathway
    • Y.Jiang, S.K.Pore, J.H.Lee, S.Sriram, B.K.Mai, D.H.Han, P.Agarwalla, A.Zakrzewska, Y.Kim, R.Banerjee, et al. Characterization of mammalian N-degrons and development of heterovalent inhibitors of the N-end rule pathway. Chem Sci 2013; 4:3339-46; http://dx.doi.org/10.1039/c3sc51059j
    • (2013) Chem Sci , vol.4 , pp. 3339-3346
    • Jiang, Y.1    Pore, S.K.2    Lee, J.H.3    Sriram, S.4    Mai, B.K.5    Han, D.H.6    Agarwalla, P.7    Zakrzewska, A.8    Kim, Y.9    Banerjee, R.10
  • 15
    • 84923287406 scopus 로고    scopus 로고
    • A neurostimulant para-chloroamphetamine inhibits the arginylation branch of the N-end rule pathway
    • 25212999
    • Y.Jiang, W.H.Choi, J.H.Lee, D.H.Han, J.H.Kim, Y.S.Chung, S.H.Kim, M.J.Lee. A neurostimulant para-chloroamphetamine inhibits the arginylation branch of the N-end rule pathway. Sci Rep 2014; 4:6344; PMID:25212999; http://dx.doi.org/10.1038/srep06344
    • (2014) Sci Rep , vol.4 , pp. 6344
    • Jiang, Y.1    Choi, W.H.2    Lee, J.H.3    Han, D.H.4    Kim, J.H.5    Chung, Y.S.6    Kim, S.H.7    Lee, M.J.8
  • 17
    • 84863623135 scopus 로고    scopus 로고
    • Characterization of arginylation branch of N-end rule pathway in G-protein-mediated proliferation and signaling of cardiomyocytes
    • 22577142
    • M.J.Lee, D.E.Kim, A.Zakrzewska, Y.D.Yoo, S.H.Kim, S.T.Kim, J.W.Seo, Y.S.Lee, G.W.Dorn, 2nd, U.Oh, et al. Characterization of arginylation branch of N-end rule pathway in G-protein-mediated proliferation and signaling of cardiomyocytes. J Biol Chem 2012; 287:24043-52; PMID:22577142; http://dx.doi.org/10.1074/jbc.M112.364117
    • (2012) J Biol Chem , vol.287 , pp. 24043-24052
    • Lee, M.J.1    Kim, D.E.2    Zakrzewska, A.3    Yoo, Y.D.4    Kim, S.H.5    Kim, S.T.6    Seo, J.W.7    Lee, Y.S.8    Dorn, G.W.9    Oh, U.10
  • 18
    • 0037025163 scopus 로고    scopus 로고
    • An essential role of N-terminal arginylation in cardiovascular development
    • 12098698
    • Y.T.Kwon, A.S.Kashina, I.V.Davydov, R.G.Hu, J.Y.An, J.W.Seo, F.Du, A.Varshavsky. An essential role of N-terminal arginylation in cardiovascular development. Science 2002; 297:96-9; PMID:12098698; http://dx.doi.org/10.1126/science.1069531
    • (2002) Science , vol.297 , pp. 96-99
    • Kwon, Y.T.1    Kashina, A.S.2    Davydov, I.V.3    Hu, R.G.4    An, J.Y.5    Seo, J.W.6    Du, F.7    Varshavsky, A.8
  • 19
    • 70649088959 scopus 로고    scopus 로고
    • Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations
    • 19915679
    • C.S.Brower, A.Varshavsky. Ablation of arginylation in the mouse N-end rule pathway:loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations. PLoS One 2009; 4:e7757; PMID:19915679; http://dx.doi.org/10.1371/journal.pone.0007757
    • (2009) PLoS One , vol.4 , pp. 7757
    • Brower, C.S.1    Varshavsky, A.2
  • 20
    • 84861214946 scopus 로고    scopus 로고
    • UBR2 of the N-end rule pathway is required for chromosome stability via histone ubiquitylation in spermatocytes and somatic cells
    • 22616001
    • J.Y.An, E.Kim, A.Zakrzewska, Y.D.Yoo, J.M.Jang, D.H.Han, M.J.Lee, J.W.Seo, Y.J.Lee, T.Y.Kim, et al. UBR2 of the N-end rule pathway is required for chromosome stability via histone ubiquitylation in spermatocytes and somatic cells. PLoS One 2012; 7:e37414; PMID:22616001; http://dx.doi.org/10.1371/journal.pone.0037414
    • (2012) PLoS One , vol.7 , pp. 37414
    • An, J.Y.1    Kim, E.2    Zakrzewska, A.3    Yoo, Y.D.4    Jang, J.M.5    Han, D.H.6    Lee, M.J.7    Seo, J.W.8    Lee, Y.J.9    Kim, T.Y.10
  • 22
    • 27144557281 scopus 로고    scopus 로고
    • The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators
    • 16222293
    • R.G.Hu, J.Sheng, X.Qi, Z.Xu, T.T.Takahashi, A.Varshavsky. The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators. Nature 2005; 437:981-6; PMID:16222293; http://dx.doi.org/10.1038/nature04027
    • (2005) Nature , vol.437 , pp. 981-986
    • Hu, R.G.1    Sheng, J.2    Qi, X.3    Xu, Z.4    Takahashi, T.T.5    Varshavsky, A.6
  • 23
    • 0032514735 scopus 로고    scopus 로고
    • Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway
    • 9770532
    • V.Solomon, V.Baracos, P.Sarraf, A.L.Goldberg. Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway. Proc Natl Acad Sci U S A 1998; 95:12602-7; PMID:9770532; http://dx.doi.org/10.1073/pnas.95.21.12602
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12602-12607
    • Solomon, V.1    Baracos, V.2    Sarraf, P.3    Goldberg, A.L.4
  • 24
    • 0032566716 scopus 로고    scopus 로고
    • The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle
    • 9737984
    • V.Solomon, S.H.Lecker, A.L.Goldberg. The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. J Biol Chem 1998; 273:25216-22; PMID:9737984; http://dx.doi.org/10.1074/jbc.273.39.25216
    • (1998) J Biol Chem , vol.273 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 25
    • 0032751546 scopus 로고    scopus 로고
    • Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
    • 10562303
    • S.H.Lecker, V.Solomon, S.R.Price, Y.T.Kwon, W.E.Mitch, A.L.Goldberg. Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. J Clin Invest 1999; 104:1411-20; PMID:10562303; http://dx.doi.org/10.1172/JCI7300
    • (1999) J Clin Invest , vol.104 , pp. 1411-1420
    • Lecker, S.H.1    Solomon, V.2    Price, S.R.3    Kwon, Y.T.4    Mitch, W.E.5    Goldberg, A.L.6
  • 26
    • 84879637332 scopus 로고    scopus 로고
    • Signaling mechanism of tumor cell-induced up-regulation of E3 ubiquitin ligase UBR2
    • 23568773
    • G.Zhang, R.K.Lin, Y.T.Kwon, Y.P.Li. Signaling mechanism of tumor cell-induced up-regulation of E3 ubiquitin ligase UBR2. FASEB J 2013; 27:2893-901; PMID:23568773; http://dx.doi.org/10.1096/fj.12-222711
    • (2013) FASEB J , vol.27 , pp. 2893-2901
    • Zhang, G.1    Lin, R.K.2    Kwon, Y.T.3    Li, Y.P.4
  • 27
    • 84876832401 scopus 로고    scopus 로고
    • Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway
    • 23499006
    • C.S.Brower, K.I.Piatkov, A.Varshavsky. Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway. Mol Cell 2013; 50:161-71; PMID:23499006; http://dx.doi.org/10.1016/j.molcel.2013.02.009
    • (2013) Mol Cell , vol.50 , pp. 161-171
    • Brower, C.S.1    Piatkov, K.I.2    Varshavsky, A.3
  • 28
    • 84924769665 scopus 로고    scopus 로고
    • Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway
    • 25766235
    • S.E.Park, J.M.Kim, O.H.Seok, H.Cho, B.Wadas, S.Y.Kim, A.Varshavsky, C.S.Hwang. Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway. Science 2015; 347:1249-52; PMID:25766235; http://dx.doi.org/10.1126/science.aaa3844
    • (2015) Science , vol.347 , pp. 1249-1252
    • Park, S.E.1    Kim, J.M.2    Seok, O.H.3    Cho, H.4    Wadas, B.5    Kim, S.Y.6    Varshavsky, A.7    Hwang, C.S.8
  • 29
    • 0033485869 scopus 로고    scopus 로고
    • The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain
    • 10581257
    • Y.Xie, A.Varshavsky. The E2-E3 interaction in the N-end rule pathway:the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain. Embo J 1999; 18:6832-44; PMID:10581257; http://dx.doi.org/10.1093/emboj/18.23.6832
    • (1999) Embo J , vol.18 , pp. 6832-6844
    • Xie, Y.1    Varshavsky, A.2
  • 30
    • 35648954603 scopus 로고    scopus 로고
    • Listeriolysin O secreted by Listeria monocytogenes into the host cell cytosol is degraded by the N-end rule pathway
    • 17682039
    • P.Schnupf, J.Zhou, A.Varshavsky, D.A.Portnoy. Listeriolysin O secreted by Listeria monocytogenes into the host cell cytosol is degraded by the N-end rule pathway. Infect Immun 2007; 75:5135-47; PMID:17682039; http://dx.doi.org/10.1128/IAI.00164-07
    • (2007) Infect Immun , vol.75 , pp. 5135-5147
    • Schnupf, P.1    Zhou, J.2    Varshavsky, A.3    Portnoy, D.A.4
  • 31
    • 84863571174 scopus 로고    scopus 로고
    • The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments
    • 22670058
    • K.I.Piatkov, C.S.Brower, A.Varshavsky. The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments. Proc Natl Acad Sci U S A 2012; 109:E1839-47; PMID:22670058; http://dx.doi.org/10.1073/pnas.1207786109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. E1839-E1847
    • Piatkov, K.I.1    Brower, C.S.2    Varshavsky, A.3
  • 32
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathway
    • 24121706
    • K.Yamano, R.J.Youle. PINK1 is degraded through the N-end rule pathway. Autophagy 2013; 9:1758-69; PMID:24121706; http://dx.doi.org/10.4161/auto.24633
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 33
    • 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
    • 23431188
    • T.Tasaki, S.T.Kim, A.Zakrzewska, B.E.Lee, M.J.Kang, Y.D.Yoo, H.J.Cha-Molstad, J.Hwang, N.K.Soung, K.S.Sung, 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 U S A 2013; 110:3800-5; PMID:23431188; http://dx.doi.org/10.1073/pnas.1217358110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 3800-3805
    • Tasaki, T.1    Kim, S.T.2    Zakrzewska, A.3    Lee, B.E.4    Kang, M.J.5    Yoo, Y.D.6    Cha-Molstad, H.J.7    Hwang, J.8    Soung, N.K.9    Sung, K.S.10
  • 34
    • 84934298725 scopus 로고    scopus 로고
    • Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding
    • 26075355
    • H.Cha-Molstad, K.S.Sung, J.Hwang, K.A.Kim, J.E.Yu, Y.D.Yoo, J.M.Jang, D.H.Han, M.Molstad, J.G.Kim, et al. Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding. Nat Cell Biol 2015; 17:917-29; PMID:26075355; http://dx.doi.org/10.1038/ncb3177
    • (2015) Nat Cell Biol , vol.17 , pp. 917-929
    • Cha-Molstad, H.1    Sung, K.S.2    Hwang, J.3    Kim, K.A.4    Yu, J.E.5    Yoo, Y.D.6    Jang, J.M.7    Han, D.H.8    Molstad, M.9    Kim, J.G.10
  • 35
    • 84878114130 scopus 로고    scopus 로고
    • Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system
    • 23528736
    • M.J.Lee, J.H.Lee, D.C.Rubinsztein. Tau degradation:the ubiquitin-proteasome system versus the autophagy-lysosome system. Prog Neurobiol 2013; 105:49-59; PMID:23528736; http://dx.doi.org/10.1016/j.pneurobio.2013.03.001
    • (2013) Prog Neurobiol , vol.105 , pp. 49-59
    • Lee, M.J.1    Lee, J.H.2    Rubinsztein, D.C.3
  • 36
    • 53549084325 scopus 로고    scopus 로고
    • Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?
    • 18758232
    • D.J.Klionsky, Z.Elazar, P.O.Seglen, D.C.Rubinsztein. Does bafilomycin A1 block the fusion of autophagosomes with lysosomes? Autophagy 2008; 4:849-50; PMID:18758232; http://dx.doi.org/10.4161/auto.6845
    • (2008) Autophagy , vol.4 , pp. 849-850
    • Klionsky, D.J.1    Elazar, Z.2    Seglen, P.O.3    Rubinsztein, D.C.4
  • 37
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • 20144757
    • N.Mizushima, T.Yoshimori, B.Levine. Methods in mammalian autophagy research. Cell 2010; 140:313-26; PMID:20144757; http://dx.doi.org/10.1016/j.cell.2010.01.028
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 38
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • 17534139
    • S.Kimura, T.Noda, T.Yoshimori. Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3. Autophagy 2007; 3:452-60; PMID:17534139; http://dx.doi.org/10.4161/auto.4451
    • (2007) Autophagy , vol.3 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 39
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • 17921520
    • S.Sarkar, G.Krishna, S.Imarisio, S.Saiki, C.J.O'Kane, D.C.Rubinsztein. A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. Hum Mol Genet 2008; 17:170-8; PMID:17921520; http://dx.doi.org/10.1093/hmg/ddm294
    • (2008) Hum Mol Genet , vol.17 , pp. 170-178
    • Sarkar, S.1    Krishna, G.2    Imarisio, S.3    Saiki, S.4    O'Kane, C.J.5    Rubinsztein, D.C.6
  • 40
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • 15146184
    • B.Ravikumar, C.Vacher, Z.Berger, J.E.Davies, S.Luo, L.G.Oroz, F.Scaravilli, D.F.Easton, R.Duden, C.J.O'Kane, et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 2004; 36:585-95; PMID:15146184; http://dx.doi.org/10.1038/ng1362
    • (2004) Nat Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6    Scaravilli, F.7    Easton, D.F.8    Duden, R.9    O'Kane, C.J.10
  • 42
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • 14699058
    • N.Mizushima, A.Yamamoto, M.Matsui, T.Yoshimori, Y.Ohsumi. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 2004; 15:1101-11; PMID:14699058; http://dx.doi.org/10.1091/mbc.E03-09-0704
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 43
    • 84875758435 scopus 로고    scopus 로고
    • Development and characterization of monomeric N-end rule inhibitors through in vitro model substrates
    • 23432203
    • S.Sriram, J.H.Lee, B.K.Mai, Y.Jiang, Y.Kim, Y.D.Yoo, R.Banerjee, S.H.Lee, M.J.Lee. Development and characterization of monomeric N-end rule inhibitors through in vitro model substrates. J Med Chem 2013; 56:2540-6; PMID:23432203; http://dx.doi.org/10.1021/jm400046q
    • (2013) J Med Chem , vol.56 , pp. 2540-2546
    • Sriram, S.1    Lee, J.H.2    Mai, B.K.3    Jiang, Y.4    Kim, Y.5    Yoo, Y.D.6    Banerjee, R.7    Lee, S.H.8    Lee, M.J.9
  • 44
    • 33646573377 scopus 로고    scopus 로고
    • Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway
    • 16606826
    • J.Y.An, J.W.Seo, T.Tasaki, M.J.Lee, A.Varshavsky, Y.T.Kwon. Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway. Proc Natl Acad Sci U S A 2006; 103:6212-7; PMID:16606826; http://dx.doi.org/10.1073/pnas.0601700103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6212-6217
    • An, J.Y.1    Seo, J.W.2    Tasaki, T.3    Lee, M.J.4    Varshavsky, A.5    Kwon, Y.T.6
  • 45
    • 34547117631 scopus 로고    scopus 로고
    • Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems
    • 17462990
    • T.Tasaki, R.Sohr, Z.Xia, R.Hellweg, H.Hortnagl, A.Varshavsky, Y.T.Kwon. Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. J Biol Chem 2007; 282:18510-20; PMID:17462990; http://dx.doi.org/10.1074/jbc.M701894200
    • (2007) J Biol Chem , vol.282 , pp. 18510-18520
    • Tasaki, T.1    Sohr, R.2    Xia, Z.3    Hellweg, R.4    Hortnagl, H.5    Varshavsky, A.6    Kwon, Y.T.7
  • 46
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • 10802622
    • N.P.Dantuma, K.Lindsten, R.Glas, M.Jellne, M.G.Masucci. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat Biotechnol 2000; 18:538-43; PMID:10802622; http://dx.doi.org/10.1038/75406
    • (2000) Nat Biotechnol , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 47
    • 18944390015 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induction of the Grp78/BiP promoter: activating mechanisms mediated by YY1 and its interactive chromatin modifiers
    • 15899857
    • P.Baumeister, S.Luo, W.C.Skarnes, G.Sui, E.Seto, Y.Shi, A.S.Lee. Endoplasmic reticulum stress induction of the Grp78/BiP promoter:activating mechanisms mediated by YY1 and its interactive chromatin modifiers. Mol Cell Biol 2005; 25:4529-40; PMID:15899857; http://dx.doi.org/10.1128/MCB.25.11.4529-4540.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 4529-4540
    • Baumeister, P.1    Luo, S.2    Skarnes, W.C.3    Sui, G.4    Seto, E.5    Shi, Y.6    Lee, A.S.7
  • 48
    • 84861210856 scopus 로고    scopus 로고
    • The N-end rule pathway
    • 22524314
    • T.Tasaki, S.M.Sriram, K.S.Park, Y.T.Kwon. The N-end rule pathway. Annu Rev Biochem 2012; 81:261-89; PMID:22524314; http://dx.doi.org/10.1146/annurev-biochem-051710-093308
    • (2012) Annu Rev Biochem , vol.81 , pp. 261-289
    • Tasaki, T.1    Sriram, S.M.2    Park, K.S.3    Kwon, Y.T.4
  • 49
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • 17620365
    • W.X.Ding, H.M.Ni, W.Gao, T.Yoshimori, D.B.Stolz, D.Ron, X.M.Yin. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007; 171:513-24; PMID:17620365; http://dx.doi.org/10.2353/ajpath.2007.070188
    • (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
  • 50
    • 75149175502 scopus 로고    scopus 로고
    • Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells
    • 19881538
    • K.Zhu, K.Dunner, Jr, D.J.McConkey. Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells. Oncogene 2010; 29:451-62; PMID:19881538; http://dx.doi.org/10.1038/onc.2009.343
    • (2010) Oncogene , vol.29 , pp. 451-462
    • Zhu, K.1    Dunner, K.2    McConkey, D.J.3
  • 51
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • 19250912
    • V.I.Korolchuk, A.Mansilla, F.M.Menzies, D.C.Rubinsztein. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 2009; 33:517-27; PMID:19250912; http://dx.doi.org/10.1016/j.molcel.2009.01.021
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 53
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • 16286508
    • G.Bjorkoy, T.Lamark, A.Brech, H.Outzen, M.Perander, A.Overvatn, H.Stenmark, T.Johansen. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005; 171:603-14; PMID:16286508; http://dx.doi.org/10.1083/jcb.200507002
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 54
    • 33947164372 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
    • 17318184
    • N.Bhutani, P.Venkatraman, A.L.Goldberg. Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation. EMBO J 2007; 26:1385-96; PMID:17318184; http://dx.doi.org/10.1038/sj.emboj.7601592
    • (2007) EMBO J , vol.26 , pp. 1385-1396
    • Bhutani, N.1    Venkatraman, P.2    Goldberg, A.L.3
  • 55
    • 84857058225 scopus 로고    scopus 로고
    • Control of autophagy as a therapy for neurodegenerative disease
    • H.Harris, D.C.Rubinsztein. Control of autophagy as a therapy for neurodegenerative disease. Nat Rev Neurol 2012; 8:108-17; http://dx.doi.org/10.1038/nrneurol.2011.200
    • (2012) Nat Rev Neurol , vol.8 , pp. 108-117
    • Harris, H.1    Rubinsztein, D.C.2
  • 56
    • 34447498400 scopus 로고    scopus 로고
    • Tau aggregation and toxicity in a cell culture model of tauopathy
    • 17428800
    • B.Bandyopadhyay, G.Li, H.Yin, J.Kuret. Tau aggregation and toxicity in a cell culture model of tauopathy. J Biol Chem 2007; 282:16454-64; PMID:17428800; http://dx.doi.org/10.1074/jbc.M700192200
    • (2007) J Biol Chem , vol.282 , pp. 16454-16464
    • Bandyopadhyay, B.1    Li, G.2    Yin, H.3    Kuret, J.4
  • 57
    • 84891427788 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation; lighting-up tau-tau interaction in living cells
    • 24312574
    • H.Tak, M.M.Haque, M.J.Kim, J.H.Lee, J.H.Baik, Y.Kim, D.J.Kim, R.Grailhe, Y.K.Kim. Bimolecular fluorescence complementation; lighting-up tau-tau interaction in living cells. PLoS One 2013; 8:e81682; PMID:24312574; http://dx.doi.org/10.1371/journal.pone.0081682
    • (2013) PLoS One , vol.8 , pp. 81682
    • Tak, H.1    Haque, M.M.2    Kim, M.J.3    Lee, J.H.4    Baik, J.H.5    Kim, Y.6    Kim, D.J.7    Grailhe, R.8    Kim, Y.K.9
  • 59
    • 84925763856 scopus 로고    scopus 로고
    • Oxidative stress induces caveolin 1 degradation and impairs caveolae functions in skeletal muscle cells
    • 25799323
    • A.Mougeolle, S.Poussard, M.Decossas, C.Lamaze, O.Lambert, E.Dargelos. Oxidative stress induces caveolin 1 degradation and impairs caveolae functions in skeletal muscle cells. PLoS One 2015; 10:e0122654; PMID:25799323; http://dx.doi.org/10.1371/journal.pone.0122654
    • (2015) PLoS One , vol.10 , pp. 122654
    • Mougeolle, A.1    Poussard, S.2    Decossas, M.3    Lamaze, C.4    Lambert, O.5    Dargelos, E.6
  • 60
    • 79955516080 scopus 로고    scopus 로고
    • MDC1 collaborates with TopBP1 in DNA replication checkpoint control
    • 21482717
    • J.Wang, Z.Gong, J.Chen. MDC1 collaborates with TopBP1 in DNA replication checkpoint control. J Cell Biol 2011; 193:267-73; PMID:21482717; http://dx.doi.org/10.1083/jcb.201010026
    • (2011) J Cell Biol , vol.193 , pp. 267-273
    • Wang, J.1    Gong, Z.2    Chen, J.3
  • 62
    • 24944482408 scopus 로고    scopus 로고
    • Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation
    • 16141322
    • A.Iwata, J.C.Christianson, M.Bucci, L.M.Ellerby, N.Nukina, L.S.Forno, R.R.Kopito. Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proc Natl Acad Sci U S A 2005; 102:13135-40; PMID:16141322; http://dx.doi.org/10.1073/pnas.0505801102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 13135-13140
    • Iwata, A.1    Christianson, J.C.2    Bucci, M.3    Ellerby, L.M.4    Nukina, N.5    Forno, L.S.6    Kopito, R.R.7
  • 64
    • 84960517495 scopus 로고    scopus 로고
    • Open-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation
    • 26957043
    • W.H.Choi, S.de Poot, J.H.Lee, J.H.Kim, D.H.Han, Y.K.Kim, D.Finley, M.J.Lee. Open-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation. Nat Commun 2016; 7:10963; PMID:26957043; http://dx.doi.org/10.1038/ncomms10963
    • (2016) Nat Commun , vol.7 , pp. 10963
    • Choi, W.H.1    de Poot, S.2    Lee, J.H.3    Kim, J.H.4    Han, D.H.5    Kim, Y.K.6    Finley, D.7    Lee, M.J.8
  • 65
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • 19377485
    • J.R.Wisniewski, A.Zougman, N.Nagaraj, M.Mann. Universal sample preparation method for proteome analysis. Nature Methods 2009; 6:359-62; PMID:19377485; http://dx.doi.org/10.1038/nmeth.1322
    • (2009) Nature Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 66
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: a peptide search engine integrated into the MaxQuant environment
    • 21254760
    • J.Cox, N.Neuhauser, A.Michalski, R.A.Scheltema, J.V.Olsen, M.Mann. Andromeda:a peptide search engine integrated into the MaxQuant environment. J Proteome Res 2011; 10:1794-805; PMID:21254760; http://dx.doi.org/10.1021/pr101065j
    • (2011) J Proteome Res , vol.10 , pp. 1794-1805
    • Cox, J.1    Neuhauser, N.2    Michalski, A.3    Scheltema, R.A.4    Olsen, J.V.5    Mann, M.6
  • 67
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • 19131956
    • W.Huang da, B.T.Sherman, R.A.Lempicki. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 2009; 4:44-57; PMID:19131956; http://dx.doi.org/10.1038/nprot.2008.211
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3


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