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Volumn 1833, Issue 12, 2013, Pages 2714-2724

Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation

Author keywords

Amyloid peptide; Fluorescent reporter; Protein aggregation; Protein degradation; Protein folding; Yeast

Indexed keywords

ARTICLE; CELL INCLUSION; CELL VIABILITY; CYTOPLASM; DEGENERATIVE DISEASE; FLOW CYTOMETRY; FLUORESCENCE ANALYSIS; IMMUNOBLOTTING; IN VIVO STUDY; MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; QUALITY CONTROL; SOLUBILITY;

EID: 84882799783     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.06.023     Document Type: Article
Times cited : (17)

References (68)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • Ventura S., Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol. 2006, 24:179-185.
    • (2006) Trends Biotechnol. , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 8
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson C.M. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2001, 356:133-145.
    • (2001) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 10
    • 80055086870 scopus 로고    scopus 로고
    • Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation
    • Fitzpatrick A.W., Knowles T.P., Waudby C.A., Vendruscolo M., Dobson C.M. Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation. PLoS Comput. Biol. 2011, 7:e1002169.
    • (2011) PLoS Comput. Biol. , vol.7
    • Fitzpatrick, A.W.1    Knowles, T.P.2    Waudby, C.A.3    Vendruscolo, M.4    Dobson, C.M.5
  • 11
    • 4143133235 scopus 로고    scopus 로고
    • A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins
    • Linding R., Schymkowitz J., Rousseau F., Diella F., Serrano L. A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. J. Mol. Biol. 2004, 342:345-353.
    • (2004) J. Mol. Biol. , vol.342 , pp. 345-353
    • Linding, R.1    Schymkowitz, J.2    Rousseau, F.3    Diella, F.4    Serrano, L.5
  • 12
    • 42649110014 scopus 로고    scopus 로고
    • The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case
    • Espargaro A., Castillo V., de Groot N.S., Ventura S. The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case. J. Mol. Biol. 2008, 378:1116-1131.
    • (2008) J. Mol. Biol. , vol.378 , pp. 1116-1131
    • Espargaro, A.1    Castillo, V.2    de Groot, N.S.3    Ventura, S.4
  • 13
    • 26844498710 scopus 로고    scopus 로고
    • Sequence determinants of protein aggregation: tools to increase protein solubility
    • Ventura S. Sequence determinants of protein aggregation: tools to increase protein solubility. Microb. Cell Factories 2005, 4:11.
    • (2005) Microb. Cell Factories , vol.4 , pp. 11
    • Ventura, S.1
  • 15
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F., Stefani M., Taddei N., Ramponi G., Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003, 424:805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 16
    • 79960005237 scopus 로고    scopus 로고
    • Prediction of amyloid aggregation in vivo
    • Belli M., Ramazzotti M., Chiti F. Prediction of amyloid aggregation in vivo. EMBO Rep. 2011, 12:657-663.
    • (2011) EMBO Rep. , vol.12 , pp. 657-663
    • Belli, M.1    Ramazzotti, M.2    Chiti, F.3
  • 17
    • 79957809655 scopus 로고    scopus 로고
    • Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes
    • Castillo V., Grana-Montes R., Sabate R., Ventura S. Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes. Biotechnol. J. 2011, 6:674-685.
    • (2011) Biotechnol. J. , vol.6 , pp. 674-685
    • Castillo, V.1    Grana-Montes, R.2    Sabate, R.3    Ventura, S.4
  • 18
    • 84876041730 scopus 로고    scopus 로고
    • Breaking the amyloidogenicity code: methods to predict amyloids from amino acid sequence
    • Ahmed A.B., Kajava A.V. Breaking the amyloidogenicity code: methods to predict amyloids from amino acid sequence. FEBS Lett. 2013, 587:1089-1095.
    • (2013) FEBS Lett. , vol.587 , pp. 1089-1095
    • Ahmed, A.B.1    Kajava, A.V.2
  • 19
    • 84871439110 scopus 로고    scopus 로고
    • Bioinformatics aggregation predictors in the study of protein conformational diseases of the human nervous system
    • Guidolin D., Agnati L.F., Albertin G., Tortorella C., Fuxe K. Bioinformatics aggregation predictors in the study of protein conformational diseases of the human nervous system. Electrophoresis 2012, 33:3669-3679.
    • (2012) Electrophoresis , vol.33 , pp. 3669-3679
    • Guidolin, D.1    Agnati, L.F.2    Albertin, G.3    Tortorella, C.4    Fuxe, K.5
  • 20
    • 33644940173 scopus 로고    scopus 로고
    • Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
    • de Groot N.S., Aviles F.X., Vendrell J., Ventura S. Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J. 2006, 273:658-668.
    • (2006) FEBS J. , vol.273 , pp. 658-668
    • de Groot, N.S.1    Aviles, F.X.2    Vendrell, J.3    Ventura, S.4
  • 21
    • 33745991934 scopus 로고    scopus 로고
    • Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
    • de Groot N.S., Ventura S. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J. Biotechnol. 2006, 125:110-113.
    • (2006) J. Biotechnol. , vol.125 , pp. 110-113
    • de Groot, N.S.1    Ventura, S.2
  • 24
    • 53949113122 scopus 로고    scopus 로고
    • Kinetic and thermodynamic stability of bacterial intracellular aggregates
    • Espargaro A., Sabate R., Ventura S. Kinetic and thermodynamic stability of bacterial intracellular aggregates. FEBS Lett. 2008, 582:3669-3673.
    • (2008) FEBS Lett. , vol.582 , pp. 3669-3673
    • Espargaro, A.1    Sabate, R.2    Ventura, S.3
  • 26
    • 77952741735 scopus 로고    scopus 로고
    • Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?
    • Khurana V., Lindquist S. Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?. Nat. Rev. Neurosci. 2010, 11:436-449.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 436-449
    • Khurana, V.1    Lindquist, S.2
  • 27
    • 78349294528 scopus 로고    scopus 로고
    • Simple is good: yeast models of neurodegeneration
    • Tenreiro S., Outeiro T.F. Simple is good: yeast models of neurodegeneration. FEMS Yeast Res. 2010, 10:970-979.
    • (2010) FEMS Yeast Res. , vol.10 , pp. 970-979
    • Tenreiro, S.1    Outeiro, T.F.2
  • 29
    • 84872085620 scopus 로고    scopus 로고
    • A yeast model for amyloid-beta aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity
    • D'Angelo F., Vignaud H., Di Martino J., Salin B., Devin A., Cullin C., Marchal C. A yeast model for amyloid-beta aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity. Dis. Model. Mech. 2013, 6:206-216.
    • (2013) Dis. Model. Mech. , vol.6 , pp. 206-216
    • D'Angelo, F.1    Vignaud, H.2    Di Martino, J.3    Salin, B.4    Devin, A.5    Cullin, C.6    Marchal, C.7
  • 31
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • Outeiro T.F., Lindquist S. Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 2003, 302:1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 32
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S., Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:1589-1594.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 33
    • 0345189365 scopus 로고    scopus 로고
    • Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein
    • Willingham S., Outeiro T.F., DeVit M.J., Lindquist S.L., Muchowski P.J. Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 2003, 302:1769-1772.
    • (2003) Science , vol.302 , pp. 1769-1772
    • Willingham, S.1    Outeiro, T.F.2    DeVit, M.J.3    Lindquist, S.L.4    Muchowski, P.J.5
  • 34
    • 84887107990 scopus 로고    scopus 로고
    • Harnessing the power of yeast to unravel the molecular basis of neurodegeneration
    • Tenreiro S., Munder M.C., Alberti S., Outeiro T.F. Harnessing the power of yeast to unravel the molecular basis of neurodegeneration. J. Neurochem. 2013, 10.1111/jnc.1227.
    • (2013) J. Neurochem.
    • Tenreiro, S.1    Munder, M.C.2    Alberti, S.3    Outeiro, T.F.4
  • 35
    • 0025974219 scopus 로고
    • Tackling the protease problem in Saccharomyces cerevisiae
    • Jones E.W. Tackling the protease problem in Saccharomyces cerevisiae. Methods Enzymol. 1991, 194:428-453.
    • (1991) Methods Enzymol. , vol.194 , pp. 428-453
    • Jones, E.W.1
  • 37
    • 0041816383 scopus 로고    scopus 로고
    • Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization
    • Bitan G., Vollers S.S., Teplow D.B. Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization. J. Biol. Chem. 2003, 278:34882-34889.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34882-34889
    • Bitan, G.1    Vollers, S.S.2    Teplow, D.B.3
  • 38
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator method for predicting protein aggregation propensities
    • Tartaglia G.G., Vendruscolo M. The Zyggregator method for predicting protein aggregation propensities. Chem. Soc. Rev. 2008, 37:1395-1401.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 39
    • 77949532822 scopus 로고    scopus 로고
    • FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence
    • Garbuzynskiy S.O., Lobanov M.Y., Galzitskaya O.V. FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence. Bioinformatics 2010, 26:326-332.
    • (2010) Bioinformatics , vol.26 , pp. 326-332
    • Garbuzynskiy, S.O.1    Lobanov, M.Y.2    Galzitskaya, O.V.3
  • 40
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22:1302-1306.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 41
    • 33750010673 scopus 로고    scopus 로고
    • Modulation of Abeta42 low-n oligomerization using a novel yeast reporter system
    • Bagriantsev S., Liebman S. Modulation of Abeta42 low-n oligomerization using a novel yeast reporter system. BMC Biol. 2006, 4:32.
    • (2006) BMC Biol. , vol.4 , pp. 32
    • Bagriantsev, S.1    Liebman, S.2
  • 44
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006, 443:780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 45
    • 84859827831 scopus 로고    scopus 로고
    • The proteasome: molecular machinery and pathophysiological roles
    • Tanaka K., Mizushima T., Saeki Y. The proteasome: molecular machinery and pathophysiological roles. Biol. Chem. 2012, 393:217-234.
    • (2012) Biol. Chem. , vol.393 , pp. 217-234
    • Tanaka, K.1    Mizushima, T.2    Saeki, Y.3
  • 47
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein D.C., Codogno P., Levine B. Autophagy modulation as a potential therapeutic target for diverse diseases. Nat. Rev. Drug Discov. 2012, 11:709-730.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 48
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008, 454:1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 49
    • 84864979359 scopus 로고    scopus 로고
    • Aggregate clearance of alpha-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome
    • Petroi D., Popova B., Taheri-Talesh N., Irniger S., Shahpasandzadeh H., Zweckstetter M., Outeiro T.F., Braus G.H. Aggregate clearance of alpha-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome. J. Biol. Chem. 2012, 287:27567-27579.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27567-27579
    • Petroi, D.1    Popova, B.2    Taheri-Talesh, N.3    Irniger, S.4    Shahpasandzadeh, H.5    Zweckstetter, M.6    Outeiro, T.F.7    Braus, G.H.8
  • 50
    • 0030983504 scopus 로고    scopus 로고
    • Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae
    • Matsuura A., Tsukada M., Wada Y., Ohsumi Y. Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae. Gene 1997, 192:245-250.
    • (1997) Gene , vol.192 , pp. 245-250
    • Matsuura, A.1    Tsukada, M.2    Wada, Y.3    Ohsumi, Y.4
  • 51
    • 0022755757 scopus 로고
    • The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
    • Woolford C.A., Daniels L.B., Park F.J., Jones E.W., Van Arsdell J.N., Innis M.A. The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases. Mol. Cell. Biol. 1986, 6:2500-2510.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2500-2510
    • Woolford, C.A.1    Daniels, L.B.2    Park, F.J.3    Jones, E.W.4    Van Arsdell, J.N.5    Innis, M.A.6
  • 52
    • 0037134913 scopus 로고    scopus 로고
    • ERG6 and PDR5 regulate small lipophilic drug accumulation in yeast cells via distinct mechanisms
    • Emter R., Heese-Peck A., Kralli A. ERG6 and PDR5 regulate small lipophilic drug accumulation in yeast cells via distinct mechanisms. FEBS Lett. 2002, 521:57-61.
    • (2002) FEBS Lett. , vol.521 , pp. 57-61
    • Emter, R.1    Heese-Peck, A.2    Kralli, A.3
  • 53
    • 0036270964 scopus 로고    scopus 로고
    • Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae
    • Jones E.W. Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae. Methods Enzymol. 2002, 351:127-150.
    • (2002) Methods Enzymol. , vol.351 , pp. 127-150
    • Jones, E.W.1
  • 54
    • 0042322394 scopus 로고    scopus 로고
    • Autophagy in yeast: a TOR-mediated response to nutrient starvation
    • Kamada Y., Sekito T., Ohsumi Y. Autophagy in yeast: a TOR-mediated response to nutrient starvation. Curr. Top. Microbiol. Immunol. 2004, 279:73-84.
    • (2004) Curr. Top. Microbiol. Immunol. , vol.279 , pp. 73-84
    • Kamada, Y.1    Sekito, T.2    Ohsumi, Y.3
  • 55
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: valuable new tools for cell biologists
    • Lee D.H., Goldberg A.L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 1998, 8:397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 56
    • 0037102362 scopus 로고    scopus 로고
    • Protein-misfolding diseases: getting out of shape
    • Dobson C.M. Protein-misfolding diseases: getting out of shape. Nature 2002, 418:729-730.
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1
  • 58
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000, 10:524-530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 61
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • Chou P.Y., Fasman G.D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 1974, 13:211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 63
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley W.C., Creamer T.P., White S.H. Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry 1996, 35:5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 64
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 1996, 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 66
    • 84863723691 scopus 로고    scopus 로고
    • Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation
    • Fredrickson E.K., Gardner R.G. Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation. Semin. Cell Dev. Biol. 2012, 23:530-537.
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 530-537
    • Fredrickson, E.K.1    Gardner, R.G.2
  • 67
    • 4344583898 scopus 로고    scopus 로고
    • Involvement of macroautophagy in the dissolution of neuronal inclusions
    • Rideout H.J., Lang-Rollin I., Stefanis L. Involvement of macroautophagy in the dissolution of neuronal inclusions. Int. J. Biochem. Cell Biol. 2004, 36:2551-2562.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2551-2562
    • Rideout, H.J.1    Lang-Rollin, I.2    Stefanis, L.3
  • 68
    • 84863895754 scopus 로고    scopus 로고
    • Chemical biology: greasy tags for protein removal
    • Neklesa T.K., Crews C.M. Chemical biology: greasy tags for protein removal. Nature 2012, 487:308-309.
    • (2012) Nature , vol.487 , pp. 308-309
    • Neklesa, T.K.1    Crews, C.M.2


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