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Volumn 13, Issue , 2007, Pages 854-861

Confocal fluorescence resonance energy transfer microscopy study of protein-protein interactions of lens crystallins in living cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; BETA CRYSTALLIN B2; CRYSTALLIN; CYTOSKELETON PROTEIN; GAMMA CRYSTALLIN; GAMMA CRYSTALLIN C; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; RED FLUORESCENT PROTEIN; UNCLASSIFIED DRUG;

EID: 34250661067     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (17)

References (38)
  • 2
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M, Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 1983; 302:415-7.
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 3
    • 33748754289 scopus 로고    scopus 로고
    • Role of short-range protein interactions in lens opacifications
    • Ponce A, Sorensen C, Takemoto, L. Role of short-range protein interactions in lens opacifications. Mol Vis 2006; 12:879-84.
    • (2006) Mol Vis , vol.12 , pp. 879-884
    • Ponce, A.1    Sorensen, C.2    Takemoto, L.3
  • 5
    • 0025832120 scopus 로고
    • Interaction and aggregation of lens crystallins
    • Liang JN, Li XY. Interaction and aggregation of lens crystallins. Exp Eye Res 1991; 53:61-6.
    • (1991) Exp Eye Res , vol.53 , pp. 61-66
    • Liang, J.N.1    Li, X.Y.2
  • 6
    • 0037064015 scopus 로고    scopus 로고
    • Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii
    • Bova MP, Huang Q, Ding L, Horwitz J. Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. J Biol Chem 2002; 277:38468-75.
    • (2002) J Biol Chem , vol.277 , pp. 38468-38475
    • Bova, M.P.1    Huang, Q.2    Ding, L.3    Horwitz, J.4
  • 7
    • 33745712767 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants
    • Liang JJ, Liu BF. Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants. Protein Sci 2006; 15:1619-27.
    • (2006) Protein Sci , vol.15 , pp. 1619-1627
    • Liang, J.J.1    Liu, B.F.2
  • 8
    • 26244448247 scopus 로고    scopus 로고
    • Interaction of lens alpha and gamma crystallins during aging of the bovine lens
    • Peterson J, Radke G, Takemoto L. Interaction of lens alpha and gamma crystallins during aging of the bovine lens. Exp Eye Res 2005; 81:680-9.
    • (2005) Exp Eye Res , vol.81 , pp. 680-689
    • Peterson, J.1    Radke, G.2    Takemoto, L.3
  • 9
    • 26244467029 scopus 로고    scopus 로고
    • Screening of crystallin-crystallin interactions using microequilibrium dialysis
    • Ponce A, Takemoto L. Screening of crystallin-crystallin interactions using microequilibrium dialysis. Mol Vis 2005; 11:752-7.
    • (2005) Mol Vis , vol.11 , pp. 752-757
    • Ponce, A.1    Takemoto, L.2
  • 10
    • 10844246436 scopus 로고    scopus 로고
    • AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin
    • Sreelakshmi Y, Santhoshkumar P, Bhattacharyya J, Sharma KK. AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin. Biochemistry 2004; 43:15785-95.
    • (2004) Biochemistry , vol.43 , pp. 15785-15795
    • Sreelakshmi, Y.1    Santhoshkumar, P.2    Bhattacharyya, J.3    Sharma, K.K.4
  • 11
    • 14144255401 scopus 로고    scopus 로고
    • Insights into the domains required for dimerization and assembly of human alphaB crystallin
    • Ghosh JG, Clark JI. Insights into the domains required for dimerization and assembly of human alphaB crystallin. Protein Sci 2005; 14:684-95.
    • (2005) Protein Sci , vol.14 , pp. 684-695
    • Ghosh, J.G.1    Clark, J.I.2
  • 12
    • 0037040277 scopus 로고    scopus 로고
    • Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay
    • Fu L, Liang JJ. Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay. J Biol Chem 2002; 277:4255-60.
    • (2002) J Biol Chem , vol.277 , pp. 4255-4260
    • Fu, L.1    Liang, J.J.2
  • 13
    • 0032561319 scopus 로고    scopus 로고
    • Negative charges in the C-terminal domain stabilize the alphaB-crystallin complex
    • Boelens WC, Croes Y, de Ruwe M, de Reu L, de Jong WW. Negative charges in the C-terminal domain stabilize the alphaB-crystallin complex. J Biol Chem 1998; 273:28085-90.
    • (1998) J Biol Chem , vol.273 , pp. 28085-28090
    • Boelens, W.C.1    Croes, Y.2    de Ruwe, M.3    de Reu, L.4    de Jong, W.W.5
  • 14
    • 0037336078 scopus 로고    scopus 로고
    • Alteration of protein-protein interactions of congenital cataract crystallin mutants
    • Fu L, Liang JJ. Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest Ophthalmol Vis Sci 2003; 44:1155-9.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 1155-1159
    • Fu, L.1    Liang, J.J.2
  • 15
    • 25444524072 scopus 로고    scopus 로고
    • Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant
    • Liu BF, Liang JJ. Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant. Mol Vis 2005; 11:321-7.
    • (2005) Mol Vis , vol.11 , pp. 321-327
    • Liu, B.F.1    Liang, J.J.2
  • 16
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia Z, Liu Y. Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys J 2001; 81:2395-402.
    • (2001) Biophys J , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 17
    • 0035207924 scopus 로고    scopus 로고
    • Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells
    • Trinkle-Mulcahy L, Sleeman JE, Lamond AI. Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J Cell Sci 2001; 114:4219-28.
    • (2001) J Cell Sci , vol.114 , pp. 4219-4228
    • Trinkle-Mulcahy, L.1    Sleeman, J.E.2    Lamond, A.I.3
  • 18
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • Wu P, Brand L. Resonance energy transfer: methods and applications. Anal Biochem 1994; 218:1-13.
    • (1994) Anal Biochem , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 20
    • 0032479355 scopus 로고    scopus 로고
    • Subunit exchange of lens alpha-crystallin: A fluorescence energy transfer study with the fluorescent labeled alphaA-crystallin mutant W9F as a probe
    • Sun TX, Akhtar NJ, Liang JJ. Subunit exchange of lens alpha-crystallin: a fluorescence energy transfer study with the fluorescent labeled alphaA-crystallin mutant W9F as a probe. FEBS Lett 1998; 430:401-4.
    • (1998) FEBS Lett , vol.430 , pp. 401-404
    • Sun, T.X.1    Akhtar, N.J.2    Liang, J.J.3
  • 21
    • 0034719154 scopus 로고    scopus 로고
    • Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts
    • Cobb BA, Petrash JM. Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts. Biochemistry 2000; 39:15791-8.
    • (2000) Biochemistry , vol.39 , pp. 15791-15798
    • Cobb, B.A.1    Petrash, J.M.2
  • 22
    • 0038529737 scopus 로고    scopus 로고
    • Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins
    • Putilina T, Skouri-Panet F, Prat K, Lubsen NH, Tardieu A. Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins. J Biol Chem 2003; 278:13747-56.
    • (2003) J Biol Chem , vol.278 , pp. 13747-13756
    • Putilina, T.1    Skouri-Panet, F.2    Prat, K.3    Lubsen, N.H.4    Tardieu, A.5
  • 23
    • 25444512697 scopus 로고    scopus 로고
    • Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin
    • Srinivas V, Raman B, Rao KS, Ramakrishna T, Rao ChM. Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin. Mol Vis 2005; 11:249-55.
    • (2005) Mol Vis , vol.11 , pp. 249-255
    • Srinivas, V.1    Raman, B.2    Rao, K.S.3    Ramakrishna, T.4    Rao, C.M.5
  • 24
    • 0035789827 scopus 로고    scopus 로고
    • Spectroscopic analysis of lens recombinant betaB2-and gammaC-crystallin
    • Fu L, Liang JJ. Spectroscopic analysis of lens recombinant betaB2-and gammaC-crystallin. Mol Vis 2001; 7:178-83.
    • (2001) Mol Vis , vol.7 , pp. 178-183
    • Fu, L.1    Liang, J.J.2
  • 25
    • 0031962334 scopus 로고    scopus 로고
    • Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin
    • Sun TX, Liang JJ. Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin. J Biol Chem 1998; 273:286-90.
    • (1998) J Biol Chem , vol.273 , pp. 286-290
    • Sun, T.X.1    Liang, J.J.2
  • 26
    • 33745587790 scopus 로고    scopus 로고
    • In vivo heteromer formation. Expression of soluble betaA4-crystallin requires coexpression of a heteromeric partner
    • Marin-Vinader L, Onnekink C, van Genesen ST, Slingsby C, Lubsen NH. In vivo heteromer formation. Expression of soluble betaA4-crystallin requires coexpression of a heteromeric partner. FEBS J 2006; 273:3172-82.
    • (2006) FEBS J , vol.273 , pp. 3172-3182
    • Marin-Vinader, L.1    Onnekink, C.2    van Genesen, S.T.3    Slingsby, C.4    Lubsen, N.H.5
  • 27
    • 16544382615 scopus 로고    scopus 로고
    • The IXI/V motif in the C-terminal extension of alpha-crystallins: Alternative interactions and oligomeric assemblies
    • Pasta SY, Raman B, Ramakrishna T, Rao ChM. The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies. Mol Vis 2004; 10:655-62.
    • (2004) Mol Vis , vol.10 , pp. 655-662
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 28
    • 4344708041 scopus 로고    scopus 로고
    • Interactions and chaperone function of alphaA-crystallin with T5P gammaC-crystallin mutant
    • Liang JJ. Interactions and chaperone function of alphaA-crystallin with T5P gammaC-crystallin mutant. Protein Sci 2004; 13:2476-82.
    • (2004) Protein Sci , vol.13 , pp. 2476-2482
    • Liang, J.J.1
  • 29
    • 0036290404 scopus 로고    scopus 로고
    • Decreased subunit exchange of heat-treated lens alphaA-crystallin
    • Liang JJ, Fu L. Decreased subunit exchange of heat-treated lens alphaA-crystallin. Biochem Biophys Res Commun 2002; 293:7-12.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 7-12
    • Liang, J.J.1    Fu, L.2
  • 30
    • 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
    • Bova MP, McHaourab HS, Han Y, Fung BK. 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 2000; 275:1035-42.
    • (2000) J Biol Chem , vol.275 , pp. 1035-1042
    • Bova, M.P.1    McHaourab, H.S.2    Han, Y.3    Fung, B.K.4
  • 31
    • 33750142707 scopus 로고    scopus 로고
    • Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: Does deamidation contribute to crystallin insolubility?
    • Wilmarth PA, Tanner S, Dasari S, Nagalla SR, Riviere MA, Bafna V, Pevzner PA, David LL. Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility? J Proteome Res 2006; 5:2554-66.
    • (2006) J Proteome Res , vol.5 , pp. 2554-2566
    • Wilmarth, P.A.1    Tanner, S.2    Dasari, S.3    Nagalla, S.R.4    Riviere, M.A.5    Bafna, V.6    Pevzner, P.A.7    David, L.L.8
  • 32
    • 33644858451 scopus 로고    scopus 로고
    • Deamidation in human lens betaB2-crystallin destabilizes the dimer
    • Lampi KJ, Amyx KK, Ahmann P, Steel EA. Deamidation in human lens betaB2-crystallin destabilizes the dimer. Biochemistry 2006; 45:3146-53.
    • (2006) Biochemistry , vol.45 , pp. 3146-3153
    • Lampi, K.J.1    Amyx, K.K.2    Ahmann, P.3    Steel, E.A.4
  • 33
    • 33750078696 scopus 로고    scopus 로고
    • Glutamine deamidation destabilizes human gammaD-crystallin and lowers the kinetic barrier to unfolding
    • Flaugh SL, Mills IA, King J. Glutamine deamidation destabilizes human gammaD-crystallin and lowers the kinetic barrier to unfolding. J Biol Chem 2006; 281:30782-93.
    • (2006) J Biol Chem , vol.281 , pp. 30782-30793
    • Flaugh, S.L.1    Mills, I.A.2    King, J.3
  • 34
    • 0037473751 scopus 로고    scopus 로고
    • BetaB2-crystallin undergoes extensive truncation during aging in human lenses
    • Srivastava OP, Srivastava K. BetaB2-crystallin undergoes extensive truncation during aging in human lenses. Biochem Biophys Res Commun 2003; 301:44-9.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 44-49
    • Srivastava, O.P.1    Srivastava, K.2
  • 35
    • 0036784934 scopus 로고    scopus 로고
    • Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses
    • Thampi P, Hassan A, Smith JB, Abraham EC. Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses. Invest Ophthalmol Vis Sci 2002; 43:3265-72.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 3265-3272
    • Thampi, P.1    Hassan, A.2    Smith, J.B.3    Abraham, E.C.4
  • 36
    • 17644408766 scopus 로고    scopus 로고
    • Subunit exchange of polydisperse proteins: Mass spectrometry reveals consequences of alphaA-crystallin truncation
    • Aquilina JA, Benesch JL, Ding LL, Yaron O, Horwitz J, Robinson CV. Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation. J Biol Chem 2005; 280:14485-91.
    • (2005) J Biol Chem , vol.280 , pp. 14485-14491
    • Aquilina, J.A.1    Benesch, J.L.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 38
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova MP, Yaron O, Huang Q, Ding L, Haley DA, Stewart PL, Horwitz J. Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci U S A 1999; 96:6137-42.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.