메뉴 건너뛰기




Volumn 55, Issue 1, 2014, Pages 15-30

A cellular system that degrades misfolded proteins and protects against neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

POLYGLUTAMINE; PROMYELOCYTIC LEUKEMIA PROTEIN; SUMO PROTEIN; UBIQUITIN LIGASE RNF4; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84903691140     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.04.030     Document Type: Article
Times cited : (150)

References (41)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch W.E., Morimoto R.I., Dillin A., Kelly J.W. Adapting proteostasis for disease intervention. Science 2008, 319:916-919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi R., Pandolfi P.P. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol. Cell Biol. 2007, 8:1006-1016.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 3
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
    • Buchberger A., Bukau B., Sommer T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell 2010, 40:238-252.
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 6
    • 79952281303 scopus 로고    scopus 로고
    • SUMO E3 ligase activity of TRIM proteins
    • Chu Y., Yang X. SUMO E3 ligase activity of TRIM proteins. Oncogene 2011, 30:1108-1116.
    • (2011) Oncogene , vol.30 , pp. 1108-1116
    • Chu, Y.1    Yang, X.2
  • 7
    • 0030864463 scopus 로고    scopus 로고
    • Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations
    • Clark H.B., Burright E.N., Yunis W.S., Larson S., Wilcox C., Hartman B., Matilla A., Zoghbi H.Y., Orr H.T. Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations. J.Neurosci. 1997, 17:7385-7395.
    • (1997) J.Neurosci. , vol.17 , pp. 7385-7395
    • Clark, H.B.1    Burright, E.N.2    Yunis, W.S.3    Larson, S.4    Wilcox, C.5    Hartman, B.6    Matilla, A.7    Zoghbi, H.Y.8    Orr, H.T.9
  • 8
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings C.J., Reinstein E., Sun Y., Antalffy B., Jiang Y., Ciechanover A., Orr H.T., Beaudet A.L., Zoghbi H.Y. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 1999, 24:879-892.
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 9
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng M., Hochstrasser M. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature 2006, 443:827-831.
    • (2006) Nature , vol.443 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 10
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 2003, 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 11
    • 78650441363 scopus 로고    scopus 로고
    • Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins
    • Fiumara F., Fioriti L., Kandel E.R., Hendrickson W.A. Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins. Cell 2010, 143:1121-1135.
    • (2010) Cell , vol.143 , pp. 1121-1135
    • Fiumara, F.1    Fioriti, L.2    Kandel, E.R.3    Hendrickson, W.A.4
  • 12
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • Gardner R.G., Nelson Z.W., Gottschling D.E. Degradation-mediated protein quality control in the nucleus. Cell 2005, 120:803-815.
    • (2005) Cell , vol.120 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 13
    • 79956017557 scopus 로고    scopus 로고
    • Partial loss of Tip60 slows mid-stage neurodegeneration in a spinocerebellar ataxia type 1 (SCA1) mouse model
    • Gehrking K.M., Andresen J.M., Duvick L., Lough J., Zoghbi H.Y., Orr H.T. Partial loss of Tip60 slows mid-stage neurodegeneration in a spinocerebellar ataxia type 1 (SCA1) mouse model. Hum. Mol. Genet. 2011, 20:2204-2212.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2204-2212
    • Gehrking, K.M.1    Andresen, J.M.2    Duvick, L.3    Lough, J.4    Zoghbi, H.Y.5    Orr, H.T.6
  • 14
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998, 94:73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 15
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426:895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 17
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl F.U., Bracher A., Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475:324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 21
    • 36349022018 scopus 로고    scopus 로고
    • Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction
    • Martin S., Wilkinson K.A., Nishimune A., Henley J.M. Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction. Nat. Rev. Neurosci. 2007, 8:948-959.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 948-959
    • Martin, S.1    Wilkinson, K.A.2    Nishimune, A.3    Henley, J.M.4
  • 23
  • 24
    • 54949126675 scopus 로고    scopus 로고
    • TRIM family proteins and their emerging roles in innate immunity
    • Ozato K., Shin D.M., Chang T.H., Morse H.C. TRIM family proteins and their emerging roles in innate immunity. Nat. Rev. Immunol. 2008, 8:849-860.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 849-860
    • Ozato, K.1    Shin, D.M.2    Chang, T.H.3    Morse, H.C.4
  • 25
    • 59249094982 scopus 로고    scopus 로고
    • SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems
    • Panavas T., Sanders C., Butt T.R. SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems. Methods Mol. Biol. 2009, 497:303-317.
    • (2009) Methods Mol. Biol. , vol.497 , pp. 303-317
    • Panavas, T.1    Sanders, C.2    Butt, T.R.3
  • 26
    • 20444467297 scopus 로고    scopus 로고
    • SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal
    • Riley B.E., Zoghbi H.Y., Orr H.T. SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal. J.Biol. Chem. 2005, 280:21942-21948.
    • (2005) J.Biol. Chem. , vol.280 , pp. 21942-21948
    • Riley, B.E.1    Zoghbi, H.Y.2    Orr, H.T.3
  • 27
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüdiger S., Germeroth L., Schneider-Mergener J., Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 1997, 16:1501-1507.
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 28
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh H., Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J.Biol. Chem. 2000, 275:6252-6258.
    • (2000) J.Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 30
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe D.J. Folding proteins in fatal ways. Nature 2003, 426:900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 33
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins
    • Sun H., Leverson J.D., Hunter T. Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J. 2007, 26:4102-4112.
    • (2007) EMBO J. , vol.26 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 36
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor J.P., Hardy J., Fischbeck K.H. Toxic proteins in neurodegenerative disease. Science 2002, 296:1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 37
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J., Mogk A., Bukau B. Cellular strategies for controlling protein aggregation. Nat. Rev. Mol. Cell Biol. 2010, 11:777-788.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 38
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef L.G., Lindsten K., Masucci M.G., Dantuma N.P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 2002, 11:2689-2700.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 39
    • 63049110916 scopus 로고    scopus 로고
    • Quality control of a transcriptional regulator by SUMO-targeted degradation
    • Wang Z., Prelich G. Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol. Cell. Biol. 2009, 29:1694-1706.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1694-1706
    • Wang, Z.1    Prelich, G.2
  • 41
    • 77952566949 scopus 로고    scopus 로고
    • Mechanisms, regulation and consequences of protein SUMOylation
    • Wilkinson K.A., Henley J.M. Mechanisms, regulation and consequences of protein SUMOylation. Biochem. J. 2010, 428:133-145.
    • (2010) Biochem. J. , vol.428 , pp. 133-145
    • Wilkinson, K.A.1    Henley, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.