메뉴 건너뛰기




Volumn 401, Issue 5, 2010, Pages 931-939

Charge-Rich Regions Modulate the Anti-Aggregation Activity of Hsp90

Author keywords

Aggregation; Chaperone; Charge; Hsp90; Misfolding

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90;

EID: 77955551442     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.066     Document Type: Article
Times cited : (36)

References (43)
  • 1
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10:S10-S17.
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 33745167938 scopus 로고    scopus 로고
    • Protein-misfolding diseases and chaperone-based therapeutic approaches
    • Chaudhuri T.K., Paul S. Protein-misfolding diseases and chaperone-based therapeutic approaches. FEBS J. 2006, 273:1331-1349.
    • (2006) FEBS J. , vol.273 , pp. 1331-1349
    • Chaudhuri, T.K.1    Paul, S.2
  • 4
    • 47549104977 scopus 로고    scopus 로고
    • Quality control of the proteins associated with neurodegenerative diseases
    • Gao X., Hu H. Quality control of the proteins associated with neurodegenerative diseases. Acta Biochim. Biophys. Sin. (Shanghai) 2008, 40:612-618.
    • (2008) Acta Biochim. Biophys. Sin. (Shanghai) , vol.40 , pp. 612-618
    • Gao, X.1    Hu, H.2
  • 5
    • 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
  • 6
    • 24944456875 scopus 로고    scopus 로고
    • Protein misfolding, aggregation, and degradation in disease
    • Gregersen N., Bolund L., Bross P. Protein misfolding, aggregation, and degradation in disease. Mol. Biotechnol. 2005, 31:141-150.
    • (2005) Mol. Biotechnol. , vol.31 , pp. 141-150
    • Gregersen, N.1    Bolund, L.2    Bross, P.3
  • 7
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry 1990, 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 8
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson C.M. Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 2004, 15:3-16.
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 9
    • 0141746349 scopus 로고    scopus 로고
    • The role of protein stability, solubility, and net charge in amyloid fibril formation
    • Schmittschmitt J.P., Scholtz J.M. The role of protein stability, solubility, and net charge in amyloid fibril formation. Protein Sci. 2003, 12:2374-2378.
    • (2003) Protein Sci. , vol.12 , pp. 2374-2378
    • Schmittschmitt, J.P.1    Scholtz, J.M.2
  • 10
    • 3142609724 scopus 로고    scopus 로고
    • Protein aggregation during overexpression limited by peptide extensions with large net negative charge
    • Zhang Y., Howitt J., McCorkle S., Lawrence P., Springer K., Freimuth P. Protein aggregation during overexpression limited by peptide extensions with large net negative charge. Protein Expression Purif. 2004, 36:207-216.
    • (2004) Protein Expression Purif. , vol.36 , pp. 207-216
    • Zhang, Y.1    Howitt, J.2    McCorkle, S.3    Lawrence, P.4    Springer, K.5    Freimuth, P.6
  • 11
    • 34548174652 scopus 로고    scopus 로고
    • Supercharging proteins can impart unusual resilience
    • Lawrence M.S., Phillips K.J., Liu D.R. Supercharging proteins can impart unusual resilience. J. Am. Chem. Soc. 2007, 129:10110-10112.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10110-10112
    • Lawrence, M.S.1    Phillips, K.J.2    Liu, D.R.3
  • 12
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl F.U., Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 2009, 16:574-581.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 13
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • Liberek K., Lewandowska A., Zietkiewicz S. Chaperones in control of protein disaggregation. EMBO J. 2008, 27:328-335.
    • (2008) EMBO J. , vol.27 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 14
    • 25444522227 scopus 로고    scopus 로고
    • Molecular chaperones in protein quality control
    • Lee S., Tsai F.T. Molecular chaperones in protein quality control. J. Biochem. Mol. Biol. 2005, 38:259-265.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 259-265
    • Lee, S.1    Tsai, F.T.2
  • 16
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology
    • Feder M.E., Hofmann G.E. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol. 1999, 61:243-282.
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 17
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., Horwich A.L., Sigler P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 1997, 388:741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 19
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl L.H., Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75:271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 20
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 2005, 62:670-684.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 21
    • 66649131702 scopus 로고    scopus 로고
    • Redox-regulated chaperones
    • Kumsta C., Jakob U. Redox-regulated chaperones. Biochemistry 2009, 48:4666-4676.
    • (2009) Biochemistry , vol.48 , pp. 4666-4676
    • Kumsta, C.1    Jakob, U.2
  • 22
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob U., Lilie H., Meyer I., Buchner J. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J. Biol. Chem. 1995, 270:7288-7294.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 23
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro
    • Evans C.G., Wisen S., Gestwicki J.E. Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro. J. Biol. Chem. 2006, 281:33182-33191.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisen, S.2    Gestwicki, J.E.3
  • 24
    • 10344243547 scopus 로고    scopus 로고
    • Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures
    • Muller L., Schaupp A., Walerych D., Wegele H., Buchner J. Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures. J. Biol. Chem. 2004, 279:48846-48854.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48846-48854
    • Muller, L.1    Schaupp, A.2    Walerych, D.3    Wegele, H.4    Buchner, J.5
  • 25
    • 6344275303 scopus 로고    scopus 로고
    • Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
    • Youker R.T., Walsh P., Beilharz T., Lithgow T., Brodsky J.L. Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol. Biol. Cell 2004, 15:4787-4797.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4787-4797
    • Youker, R.T.1    Walsh, P.2    Beilharz, T.3    Lithgow, T.4    Brodsky, J.L.5
  • 26
    • 0026778032 scopus 로고
    • Hsp90 chaperones protein folding in vitro
    • Wiech H., Buchner J., Zimmermann R., Jakob U. Hsp90 chaperones protein folding in vitro. Nature 1992, 358:169-170.
    • (1992) Nature , vol.358 , pp. 169-170
    • Wiech, H.1    Buchner, J.2    Zimmermann, R.3    Jakob, U.4
  • 28
    • 0031693703 scopus 로고    scopus 로고
    • The Hsp90 complex-a super-chaperone machine as a novel drug target
    • Scheibel T., Buchner J. The Hsp90 complex-a super-chaperone machine as a novel drug target. Biochem. Pharmacol. 1998, 56:675-682.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 675-682
    • Scheibel, T.1    Buchner, J.2
  • 29
    • 20144389462 scopus 로고    scopus 로고
    • Construction, verification and experimental use of two epitope-tagged collections of budding yeast strains
    • Howson R., Huh W.K., Ghaemmaghami S., Falvo J.V., Bower K., Belle A., et al. Construction, verification and experimental use of two epitope-tagged collections of budding yeast strains. Comp. Funct. Genomics 2005, 6:2-16.
    • (2005) Comp. Funct. Genomics , vol.6 , pp. 2-16
    • Howson, R.1    Huh, W.K.2    Ghaemmaghami, S.3    Falvo, J.V.4    Bower, K.5    Belle, A.6
  • 30
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman B.C., Morimoto R.I. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 1996, 15:2969-2979.
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 31
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali M.M.U., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006, 440:1013-1017.
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.U.1    Roe, S.M.2    Vaughan, C.K.3    Meyer, P.4    Panaretou, B.5    Piper, P.W.6
  • 32
    • 0030462612 scopus 로고    scopus 로고
    • Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast
    • Louvion J.F., Warth R., Picard D. Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl Acad. Sci. USA 1996, 93:13937-13942.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13937-13942
    • Louvion, J.F.1    Warth, R.2    Picard, D.3
  • 33
    • 69249130057 scopus 로고    scopus 로고
    • The charged linker region is an important regulator of Hsp90 function
    • Hainzl O., Lapina M.C., Buchner J., Richter K. The charged linker region is an important regulator of Hsp90 function. J. Biol. Chem. 2009, 284:22559-22567.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22559-22567
    • Hainzl, O.1    Lapina, M.C.2    Buchner, J.3    Richter, K.4
  • 35
    • 0029997424 scopus 로고    scopus 로고
    • Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway
    • Qu B.H., Thomas P.J. Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway. J. Biol. Chem. 1996, 271:7261-7264.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7261-7264
    • Qu, B.H.1    Thomas, P.J.2
  • 37
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions
    • Meyer P., Prodromou C., Hu B., Vaughan C., Roe S.M., Panaretou B., et al. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 2003, 11:647-658.
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6
  • 38
    • 70350759550 scopus 로고    scopus 로고
    • Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain
    • Tsutsumi S., Mollapour M., Graf C., Lee C.T., Scroggins B.T., Xu W., et al. Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nat. Struct. Mol. Biol. 2009, 16:1141-1147.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1141-1147
    • Tsutsumi, S.1    Mollapour, M.2    Graf, C.3    Lee, C.T.4    Scroggins, B.T.5    Xu, W.6
  • 39
    • 73649144525 scopus 로고    scopus 로고
    • Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo
    • Wayne N., Lai Y., Pullen L., Bolon D.N. Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo. J. Biol. Chem. 2010, 285:234-241.
    • (2010) J. Biol. Chem. , vol.285 , pp. 234-241
    • Wayne, N.1    Lai, Y.2    Pullen, L.3    Bolon, D.N.4
  • 40
    • 0023392855 scopus 로고
    • r 83,000 heat shock protein has a homologue in Escherichia coli
    • r 83,000 heat shock protein has a homologue in Escherichia coli. Proc. Natl Acad. Sci. USA 1987, 84:5177-5181.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5177-5181
    • Bardwell, J.C.1    Craig, E.A.2
  • 41
    • 36849083947 scopus 로고    scopus 로고
    • Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers
    • Wayne N., Bolon D.N. Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers. J. Biol. Chem. 2007, 282:35386-35395.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35386-35395
    • Wayne, N.1    Bolon, D.N.2
  • 43
    • 0023809599 scopus 로고
    • +-ATPase activity
    • +-ATPase activity. Methods Enzymol. 1988, 156:116-119.
    • (1988) Methods Enzymol. , vol.156 , pp. 116-119
    • Norby, J.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.