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Volumn 345, Issue 3, 2005, Pages 631-642

Self-association of a small heat shock protein

Author keywords

analytical ultracentrifugation; heat shock proteins; Hsp27; oligomerization; site directed mutagenesis

Indexed keywords

DIMER; HEAT SHOCK PROTEIN 27; HISTIDINE; HYDROCHLORIC ACID; MONOMER; OLIGOMER; SODIUM CHLORIDE; TETRAMER;

EID: 9644260484     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.056     Document Type: Article
Times cited : (63)

References (38)
  • 1
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain"
    • G.J. Caspers, J.A. Leunissen, and W.W. de Jong The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain" J. Mol. Evol. 40 1995 238 248
    • (1995) J. Mol. Evol. , vol.40 , pp. 238-248
    • Caspers, G.J.1    Leunissen, J.A.2    De Jong, W.W.3
  • 2
    • 0023935087 scopus 로고
    • Dogfish alpha-crystallin sequences. Comparison with small heat shock proteins and Schistosoma egg antigen
    • W.W. de Jong, J.A. Leunissen, P.J. Leenen, A. Zweers, and M. Versteeg Dogfish alpha-crystallin sequences. Comparison with small heat shock proteins and Schistosoma egg antigen J. Biol. Chem. 263 1988 5141 5149
    • (1988) J. Biol. Chem. , vol.263 , pp. 5141-5149
    • De Jong, W.W.1    Leunissen, J.A.2    Leenen, P.J.3    Zweers, A.4    Versteeg, M.5
  • 3
    • 0033515597 scopus 로고    scopus 로고
    • HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus
    • H. Lambert, S.J. Charette, A.F. Bernier, A. Guimond, and J. Landry HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus J. Biol. Chem. 274 1999 9378 9385
    • (1999) J. Biol. Chem. , vol.274 , pp. 9378-9385
    • Lambert, H.1    Charette, S.J.2    Bernier, A.F.3    Guimond, A.4    Landry, J.5
  • 4
    • 0033984092 scopus 로고    scopus 로고
    • Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation
    • Y. Sugiyama, A. Suzuki, M. Kishikawa, R. Akutsu, T. Hirose, and M.M. Waye Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation J. Biol. Chem. 275 2000 1095 1104
    • (2000) J. Biol. Chem. , vol.275 , pp. 1095-1104
    • Sugiyama, Y.1    Suzuki, A.2    Kishikawa, M.3    Akutsu, R.4    Hirose, T.5    Waye, M.M.6
  • 5
    • 0028984175 scopus 로고
    • 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids
    • 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids FEBS Letters 369 1995 305 310
    • (1995) FEBS Letters , vol.369 , pp. 305-310
    • Carver, J.A.1    Esposito, G.2    Schwedersky, G.3    Gaestel, M.4
  • 6
    • 0024997813 scopus 로고
    • Tissue-specific expression of the heat shock protein HSP27 during Drosophila melanogaster development
    • D. Pauli, C.H. Tonka, A. Tissieres, and A.P. Arrigo Tissue-specific expression of the heat shock protein HSP27 during Drosophila melanogaster development J. Cell. Biol. 111 1990 817 828
    • (1990) J. Cell. Biol. , vol.111 , pp. 817-828
    • Pauli, D.1    Tonka, C.H.2    Tissieres, A.3    Arrigo, A.P.4
  • 7
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • U. Jakob, M. Gaestel, K. Engel, and J. Buchner Small heat shock proteins are molecular chaperones J. Biol. Chem. 268 1993 1517 1520
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 8
    • 0028346451 scopus 로고
    • Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
    • K. Kato, K. Hasegawa, S. Goto, and Y. Inaguma Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27 J. Biol. Chem. 269 1994 11274 11278
    • (1994) J. Biol. Chem. , vol.269 , pp. 11274-11278
    • Kato, K.1    Hasegawa, K.2    Goto, S.3    Inaguma, Y.4
  • 9
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • D. Stokoe, K. Engel, D.G. Campbell, P. Cohen, and M. Gaestel Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins FEBS Letters 313 1992 307 313
    • (1992) FEBS Letters , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 10
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
    • N.B. Gusev, N.V. Bogatcheva, and S.B. Marston Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins Biochemistry (Mosc.) 67 2002 511 519
    • (2002) Biochemistry (Mosc.) , vol.67 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 12
    • 0036092428 scopus 로고    scopus 로고
    • Size matters: Of the small HSP27 and its large oligomers
    • C. Garrido Size matters: of the small HSP27 and its large oligomers Cell. Death Differ. 9 2002 483 485
    • (2002) Cell. Death Differ. , vol.9 , pp. 483-485
    • Garrido, C.1
  • 14
    • 0034643424 scopus 로고    scopus 로고
    • Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3
    • P. Pandey, R. Farber, A. Nakazawa, S. Kumar, A. Bharti, and C. Nalin Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3 Oncogene 19 2000 1975 1981
    • (2000) Oncogene , vol.19 , pp. 1975-1981
    • Pandey, P.1    Farber, R.2    Nakazawa, A.3    Kumar, S.4    Bharti, A.5    Nalin, C.6
  • 15
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of Daxx-mediated apoptosis by heat shock protein 27
    • S.J. Charette, J.N. Lavoie, H. Lambert, and J. Landry Inhibition of Daxx-mediated apoptosis by heat shock protein 27 Mol. Cell. Biol. 20 2000 7602 7612
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 16
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human alphaB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death
    • P. Mehlen, C. Kretz-Remy, X. Preville, and A.P. Arrigo Human hsp27, Drosophila hsp27 and human alphaB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death EMBO J. 15 1996 2695 2706
    • (1996) EMBO J. , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Kretz-Remy, C.2    Preville, X.3    Arrigo, A.P.4
  • 17
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • R. Benndorf, K. Hayess, S. Ryazantsev, M. Wieske, J. Behlke, and G. Lutsch Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity J. Biol. Chem. 269 1994 20780 20784
    • (1994) J. Biol. Chem. , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 19
    • 0034609765 scopus 로고    scopus 로고
    • Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo
    • J.M. Bruey, C. Paul, A. Fromentin, S. Hilpert, A.P. Arrigo, E. Solary, and C. Garrido Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo Oncogene 19 2000 4855 4863
    • (2000) Oncogene , vol.19 , pp. 4855-4863
    • Bruey, J.M.1    Paul, C.2    Fromentin, A.3    Hilpert, S.4    Arrigo, A.P.5    Solary, E.6    Garrido, C.7
  • 20
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • J.N. Lavoie, H. Lambert, E. Hickey, L.A. Weber, and J. Landry Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27 Mol. Cell. Biol. 15 1995 505 516
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 21
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • K.K. Kim, R. Kim, and S.H. Kim Crystal structure of a small heat-shock protein Nature 394 1998 595 599
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 23
    • 0033972325 scopus 로고    scopus 로고
    • Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
    • M.P. Bova, H.S. McHaourab, Y. Han, and B.K. Fung Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations J. Biol. Chem. 275 2000 1035 1042
    • (2000) J. Biol. Chem. , vol.275 , pp. 1035-1042
    • Bova, M.P.1    McHaourab, H.S.2    Han, Y.3    Fung, B.K.4
  • 25
    • 0032078745 scopus 로고    scopus 로고
    • NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins
    • J.A. Carver, and R.A. Lindner NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins Int. J. Biol. Macromol. 22 1998 197 209
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 197-209
    • Carver, J.A.1    Lindner, R.A.2
  • 26
    • 0025899328 scopus 로고
    • Supramolecular structure of the recombinant murine small heat shock protein hsp25
    • J. Behlke, G. Lutsch, M. Gaestel, and H. Bielka Supramolecular structure of the recombinant murine small heat shock protein hsp25 FEBS Letters 288 1991 119 122
    • (1991) FEBS Letters , vol.288 , pp. 119-122
    • Behlke, J.1    Lutsch, G.2    Gaestel, M.3    Bielka, H.4
  • 27
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation
    • T. Rogalla, M. Ehrnsperger, X. Preville, A. Kotlyarov, G. Lutsch, and C. Ducasse Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation J. Biol. Chem. 274 1999 18947 18956
    • (1999) J. Biol. Chem. , vol.274 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3    Kotlyarov, A.4    Lutsch, G.5    Ducasse, C.6
  • 28
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • D.A. Haley, M.P. Bova, Q.L. Huang, H.S. McHaourab, and P.L. Stewart Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies J. Mol. Biol. 298 2000 261 272
    • (2000) J. Mol. Biol. , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    McHaourab, H.S.4    Stewart, P.L.5
  • 29
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • P. Schuck On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation Anal. Biochem. 320 2003 104 124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 30
    • 0037974661 scopus 로고    scopus 로고
    • A role of HSPs in apoptosis through "protein triage"?
    • C. Garrido, and E. Solary A role of HSPs in apoptosis through "protein triage"? Cell. Death Differ. 10 2003 619 620
    • (2003) Cell. Death Differ. , vol.10 , pp. 619-620
    • Garrido, C.1    Solary, E.2
  • 31
    • 0034595066 scopus 로고    scopus 로고
    • An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties
    • Z. Guo, and L.F. Cooper An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties Biochem. Biophys. Res. Commun. 270 2000 183 189
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 183-189
    • Guo, Z.1    Cooper, L.F.2
  • 32
    • 0030826325 scopus 로고    scopus 로고
    • Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
    • M.R. Leroux, R. Melki, B. Gordon, G. Batelier, and E.P. Candido Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides J. Biol. Chem. 272 1997 24646 24656
    • (1997) J. Biol. Chem. , vol.272 , pp. 24646-24656
    • Leroux, M.R.1    Melki, R.2    Gordon, B.3    Batelier, G.4    Candido, E.P.5
  • 34
    • 0038043235 scopus 로고    scopus 로고
    • Analysis of the interaction of small heat shock proteins with unfolding proteins
    • T. Stromer, M. Ehrnsperger, M. Gaestel, and J. Buchner Analysis of the interaction of small heat shock proteins with unfolding proteins J. Biol. Chem. 278 2003 18015 18021
    • (2003) J. Biol. Chem. , vol.278 , pp. 18015-18021
    • Stromer, T.1    Ehrnsperger, M.2    Gaestel, M.3    Buchner, J.4
  • 36
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 37
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • P. Schuck, M.A. Perugini, N.R. Gonzales, G.J. Howlett, and D. Schubert Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems Biophys. J. 82 2002 1096 1111
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 38
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • M.L. Johnson, J.J. Correia, D.A. Yphantis, and H.R. Halvorson Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques Biophys. J. 36 1981 575 588
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4


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