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Volumn 108, Issue 51, 2011, Pages 20491-20496

Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; OLIGOMER;

EID: 84855480113     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111014108     Document Type: Article
Times cited : (130)

References (49)
  • 2
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins account for eye lens transparency
    • DOI 10.1038/302415a0
    • Delaye M, Tardieu A (1983) Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302:415-417. (Pubitemid 13164324)
    • (1983) Nature , vol.302 , Issue.5907 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 3
    • 0026483279 scopus 로고
    • α-crystallin can function as a molecular chaperone
    • Horwitz J (1992) α-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 89:10449-10453.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 4
    • 0017389118 scopus 로고
    • The vertebrate eye lens. A useful system for the study of fundamental biological processes on a molecular level
    • Bloemendal H (1977) The vertebrate eye lens. A useful system for the study of fundamental biological processes on a molecular level. Science 197:127-138.
    • (1977) Science , vol.197 , pp. 127-138
    • Bloemendal, H.1
  • 5
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the α-crystallin-small heat-shock protein superfamily
    • de Jong WW, Caspers GJ, Leunissen JAM (1998) Genealogy of the α-crystallin-small heat-shock protein superfamily. Int J Biol Macromol 22:151-162.
    • (1998) Int J Biol Macromol , vol.22 , pp. 151-162
    • De Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.M.3
  • 6
    • 77957841871 scopus 로고    scopus 로고
    • Independent evolution of the core domain and its flanking sequences in small heat shock proteins
    • Kriehuber T, et al. (2010) Independent evolution of the core domain and its flanking sequences in small heat shock proteins. FASEB J 24:3633-3642.
    • (2010) FASEB J , vol.24 , pp. 3633-3642
    • Kriehuber, T.1
  • 9
    • 0024521440 scopus 로고
    • αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • DOI 10.1016/0092-8674(89)90173-6
    • Iwaki T, Kuma-Iwaki A, Liem RK, Goldman JE (1989) αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57:71-78. (Pubitemid 19098869)
    • (1989) Cell , vol.57 , Issue.1 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.H.3    Goldman, J.E.4
  • 10
    • 0029060142 scopus 로고
    • The small heat-shock protein αB-crystallin as candidate auto-antigen in multiple sclerosis
    • van Noort JM(1995) The small heat-shock protein αB-crystallin as candidate auto-antigen in multiple sclerosis. Nature 375:798-801.
    • (1995) Nature , vol.375 , pp. 798-801
    • Van Noort, J.M.1
  • 12
    • 78549288555 scopus 로고    scopus 로고
    • Serine 59 phosphorylation of αB-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells
    • Launay N, Tarze A, Vicart P, Lilienbaum A (2010) Serine 59 phosphorylation of αB-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells. J Biol Chem 285:37324-37332.
    • (2010) J Biol Chem , vol.285 , pp. 37324-37332
    • Launay, N.1    Tarze, A.2    Vicart, P.3    Lilienbaum, A.4
  • 13
    • 69449107325 scopus 로고    scopus 로고
    • The eye lens chaperone α-crystallin forms defined globular assemblies
    • Peschek J, et al. (2009) The eye lens chaperone α-crystallin forms defined globular assemblies. Proc Natl Acad Sci USA 106:13272-13277.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13272-13277
    • Peschek, J.1
  • 16
    • 57649129014 scopus 로고    scopus 로고
    • Small heat shock protein activity is regulated by variable oligomeric structure
    • Benesch JLP, Ayoub M, Robinson CV, Aquilina JA (2008) Small heat shock protein activity is regulated by variable oligomeric structure. J Biol Chem 283:28513-28517.
    • (2008) J Biol Chem , vol.283 , pp. 28513-28517
    • Benesch, J.L.P.1    Ayoub, M.2    Robinson, C.V.3    Aquilina, J.A.4
  • 17
    • 0031962334 scopus 로고    scopus 로고
    • Intermolecular exchange and stabilization of recombinant human αA- and αB-crystallin
    • DOI 10.1074/jbc.273.1.286
    • Sun T-X, Liang JJ-N (1998) Intermolecular exchange and stabilization of recombinant human αA- and αB-crystallin. J Biol Chem 273:286-290. (Pubitemid 28042206)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.1 , pp. 286-290
    • Sun, T.-X.1    Liang, J.J.-N.2
  • 18
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, αB-Crystallin, has a variable quaternary structure
    • DOI 10.1006/jmbi.1997.1611
    • Haley DA, Horwitz J, Stewart PL (1998) The small heat-shock protein, αB-crystallin, has a variable quaternary structure. J Mol Biol 277:27-35. (Pubitemid 28151881)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.1 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 19
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • DOI 10.1038/29106
    • Kim KK, Kim R, Kim SH (1998) Crystal structure of a small heat-shock protein. Nature 394:595-599. (Pubitemid 28366837)
    • (1998) Nature , vol.394 , Issue.6693 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.-H.3
  • 21
    • 70149097520 scopus 로고    scopus 로고
    • Crystal structures of α-crystallin domain dimers of αB-crystallin and Hsp20
    • Bagneris C, et al. (2009) Crystal structures of α-crystallin domain dimers of αB-crystallin and Hsp20. J Mol Biol 392:1242-1252.
    • (2009) J Mol Biol , vol.392 , pp. 1242-1252
    • Bagneris, C.1
  • 22
    • 77957296137 scopus 로고    scopus 로고
    • Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function
    • Laganowsky A, et al. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci 19:1031-1043.
    • (2010) Protein Sci , vol.19 , pp. 1031-1043
    • Laganowsky, A.1
  • 23
    • 77956340380 scopus 로고    scopus 로고
    • Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers
    • Jehle S, et al. (2010) Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers. Nat Struct Mol Biol 17:1037-1042.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1037-1042
    • Jehle, S.1
  • 24
    • 79955597623 scopus 로고    scopus 로고
    • N-terminal domain of αB-crystallin provides a conformational switch for multimerization and structural heterogeneity
    • Jehle S, et al. (2011) N-terminal domain of αB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proc Natl Acad Sci USA 108:6409-6414.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6409-6414
    • Jehle, S.1
  • 25
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • Rappsilber J (2011) The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes. J Struct Biol 173:530-540.
    • (2011) J Struct Biol , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 26
    • 77149146167 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry
    • Chen ZA, et al. (2010) Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry. EMBO J 29:717-726.
    • (2010) EMBO J , vol.29 , pp. 717-726
    • Chen, Z.A.1
  • 27
    • 0026612249 scopus 로고
    • Identification by 1H-NMR spectroscopy of flexible C-terminal extensions in bovine lens α-crystallin
    • Carver JA, Aquilina JA, Truscott RJ, Ralston GB (1992) Identification by 1H-NMR spectroscopy of flexible C-terminal extensions in bovine lens α-crystallin. FEBS Lett 311:143-149.
    • (1992) FEBS Lett , vol.311 , pp. 143-149
    • Carver, J.A.1    Aquilina, J.A.2    Truscott, R.J.3    Ralston, G.B.4
  • 28
    • 16544382615 scopus 로고    scopus 로고
    • The IXI/V motif in the C-terminal extension of α-crystallins: Alternative interactions and oligomeric assemblies
    • Pasta SY, Raman B, Ramakrishna T, Rao C (2004) The IXI/V motif in the C-terminal extension of α-crystallins: Alternative interactions and oligomeric assemblies. Mol Vis 10:655-662. (Pubitemid 41358231)
    • (2004) Molecular Vision , vol.10 , pp. 655-662
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 29
    • 0141988870 scopus 로고    scopus 로고
    • Influence of the C-terminal residues on oligomerization of αA-crystallin
    • DOI 10.1021/bi030129w
    • Thampi P, Abraham EC (2003) Influence of the C-terminal residues on oligomerization of αA-crystallin. Biochemistry 42:11857-11863. (Pubitemid 37243647)
    • (2003) Biochemistry , vol.42 , Issue.40 , pp. 11857-11863
    • Thampi, P.1    Abraham, E.C.2
  • 30
    • 0030613774 scopus 로고    scopus 로고
    • Phosphorylation of αB-crystallin in response to various types of stress
    • DOI 10.1074/jbc.272.47.29934
    • Ito H, Okamoto K, Nakayama H, Isobe T, Kato K (1997) Phosphorylation of αB-crystallin in response to various types of stress. J Biol Chem 272:29934-29941. (Pubitemid 27508095)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.47 , pp. 29934-29941
    • Ito, H.1    Okamoto, K.2    Nakayama, H.3    Isobe, T.4    Kato, K.5
  • 31
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in αA-crystallin
    • DOI 10.1074/jbc.275.6.3767
    • Sharma KK, Kumar RS, Kumar GS, Quinn PT (2000) Synthesis and characterization of a peptide identified as a functional element in αA-crystallin. J Biol Chem 275:3767-3771. (Pubitemid 30094597)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3767-3771
    • Sharma, K.K.1    Kumar, R.S.2    Kumar, G.S.3    Quinn, P.T.4
  • 32
    • 33751244272 scopus 로고    scopus 로고
    • N- and C-terminal motifs in human αB crystallin play an important role in the recognition, selection, and solubilization of substrates
    • DOI 10.1021/bi061471m
    • Ghosh JG, Shenoy AK, Clark JI (2006) N- and C-terminal motifs in human αB crystallin play an important role in the recognition, selection, and solubilization of substrates. Biochemistry 45:13847-13854. (Pubitemid 44788753)
    • (2006) Biochemistry , vol.45 , Issue.46 , pp. 13847-13854
    • Ghosh, J.G.1    Shenoy Jr., A.K.2    Clark, J.I.3
  • 33
    • 33846161926 scopus 로고    scopus 로고
    • The N-terminal domain of αB-crystallin is protected from proteolysis by bound substrate
    • DOI 10.1016/j.bbrc.2006.12.176, PII S0006291X06028555
    • Aquilina JA, Watt SJ (2007) The N-terminal domain of αB-crystallin is protected from proteolysis by bound substrate. Biochem Biophys Res Commun 353:1115-1120. (Pubitemid 46080413)
    • (2007) Biochemical and Biophysical Research Communications , vol.353 , Issue.4 , pp. 1115-1120
    • Aquilina, J.A.1    Watt, S.J.2
  • 34
    • 0029956553 scopus 로고    scopus 로고
    • Effects of site-directed mutations on the chaperone-like activity of αB-crystallin
    • DOI 10.1074/jbc.271.45.28558
    • Plater ML, Goode D, Crabbe MJ (1996) Effects of site-directed mutations on the chaperone- like activity of αB-crystallin. J Biol Chem 271:28558-28566. (Pubitemid 26374679)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28558-28566
    • Plater, M.L.1    Goode, D.2    Crabbe, M.J.C.3
  • 36
    • 37349032463 scopus 로고    scopus 로고
    • Effect of Phosphorylation on αB-crystallin: Differences in Stability, Subunit Exchange and Chaperone Activity of Homo and Mixed Oligomers of ́B-Crystallin and its Phosphorylation-mimicking Mutant
    • DOI 10.1016/j.jmb.2007.11.019, PII S0022283607014799
    • Ahmad MdF, Raman B, Ramakrishna T, Rao ChM (2008) Effect of phosphorylation on αB-crystallin: Differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of áB-crystallin and its phosphorylation-mimicking mutant. J Mol Biol 375:1040-1051. (Pubitemid 350309398)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.4 , pp. 1040-1051
    • Ahmad, M..F.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 40
    • 59849129128 scopus 로고    scopus 로고
    • Abnormal assemblies and subunit exchange of αB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure
    • Michiel M, et al. (2009) Abnormal assemblies and subunit exchange of αB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure. Biochemistry 48:442-453.
    • (2009) Biochemistry , vol.48 , pp. 442-453
    • Michiel, M.1
  • 41
    • 79953253901 scopus 로고    scopus 로고
    • Crystal structure of R120G disease mutant of human αB-crystallin domain dimer shows closure of a groove
    • Clark AR, Naylor CE, Bagneris C, Keep NH, Slingsby C (2011) Crystal structure of R120G disease mutant of human αB-crystallin domain dimer shows closure of a groove. J Mol Biol 408:118-134.
    • (2011) J Mol Biol , vol.408 , pp. 118-134
    • Clark, A.R.1    Naylor, C.E.2    Bagneris, C.3    Keep, N.H.4    Slingsby, C.5
  • 43
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P (2000) Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 78:1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 44
    • 38349037648 scopus 로고    scopus 로고
    • Structural analysis of multiprotein complexes by cross-linking, mass spectrometry, and database searching
    • Maiolica A, et al. (2007) Structural analysis of multiprotein complexes by cross-linking, mass spectrometry, and database searching. Mol Cell Proteomics 6:2200-2211.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 2200-2211
    • Maiolica, A.1
  • 45
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • DOI 10.1038/nprot.2007.261, PII NPROT.2007.261
    • Rappsilber J, Mann M, Ishihama Y (2007) Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2:1896-906. (Pubitemid 47308128)
    • (2007) Nature Protocols , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 46
    • 0037317228 scopus 로고    scopus 로고
    • Stop And Go Extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • DOI 10.1021/ac026117i
    • Rappsilber J, Ishihama Y, Mann M(2003) Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal Chem 75:663-670. (Pubitemid 36176744)
    • (2003) Analytical Chemistry , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 47
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26:1367-1372.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 48
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single particle reconstructions. J Struct Biol 128:82-97. (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 49
    • 0034782444 scopus 로고    scopus 로고
    • HYDROMIC: Prediction of hydrodynamic properties of rigid macromolecular structures obtained from electron-microscopy images
    • de la Torre JG, Valpuesta JM, Carrascosa JL (2001) HYDROMIC: Prediction of hydrodynamic properties of rigid macromolecular structures obtained from electron-microscopy images. Eur Biophys J 30:457-462.
    • (2001) Eur Biophys J , vol.30 , pp. 457-462
    • De La Torre, J.G.1    Valpuesta, J.M.2    Carrascosa, J.L.3


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