메뉴 건너뛰기




Volumn 17, Issue , 2011, Pages 7-15

Cataract-causing αAG98R-crystallin mutant dissociates into monomers having chaperone activity

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; ALPHA CRYSTALLIN; BETA B2 CRYSTALLIN; BETA CRYSTALLIN; CHAPERONE; CITRATE SYNTHASE; MONOMER; UNCLASSIFIED DRUG;

EID: 79551717234     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (37)
  • 1
    • 0028023344 scopus 로고
    • Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology
    • [PMID: 7925426]
    • Groenen PJ, Merck KB, de Jong WW, Bloemendal H. Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Eur J Biochem 1994; 225:1-19. [PMID: 7925426]
    • (1994) Eur J Biochem , vol.225 , pp. 1-19
    • Groenen, P.J.1    Merck, K.B.2    de Jong, W.W.3    Bloemendal, H.4
  • 2
    • 61849111603 scopus 로고    scopus 로고
    • Alpha crystallin: The quest for a homogeneous quaternary structure
    • [PMID: 18703051]
    • Horwitz J. Alpha crystallin: the quest for a homogeneous quaternary structure. Exp Eye Res 2009; 88:190-194. [PMID: 18703051]
    • (2009) Exp Eye Res , vol.88 , pp. 190-194
    • Horwitz, J.1
  • 3
    • 0030793578 scopus 로고    scopus 로고
    • Preliminary studies on the aggregation process of alpha-crystallin
    • [PMID: 9268594]
    • Doss EW, Ward KA, Koretz JF. Preliminary studies on the aggregation process of alpha-crystallin. Exp Eye Res 1997; 65:255-266. [PMID: 9268594]
    • (1997) Exp Eye Res , vol.65 , pp. 255-266
    • Doss, E.W.1    Ward, K.A.2    Koretz, J.F.3
  • 4
    • 44849103123 scopus 로고    scopus 로고
    • Truncation of alphaBcrystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells
    • [PMID: 18230612]
    • Hayes VH, Devlin G, Quinlan RA. Truncation of alphaBcrystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells. J Biol Chem 2008; 283:10500-10512. [PMID: 18230612]
    • (2008) J Biol Chem , vol.283 , pp. 10500-10512
    • Hayes, V.H.1    Devlin, G.2    Quinlan, R.A.3
  • 5
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • [PMID: 1438232]
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992; 89:10449-10453. [PMID: 1438232]
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 6
    • 0030725582 scopus 로고    scopus 로고
    • The crystallins: Genes, proteins and diseases
    • [PMID: 9426193]
    • Graw J. The crystallins: genes, proteins and diseases. Biol Chem 1997; 378:1331-1348. [PMID: 9426193]
    • (1997) Biol Chem , vol.378 , pp. 1331-1348
    • Graw, J.1
  • 7
    • 33745913948 scopus 로고    scopus 로고
    • Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family
    • [PMID: 16862070]
    • Santhiya ST, Soker T, Klopp N, Illig T, Prakash MV, Selvaraj B, Gopinath PM, Graw J. Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family. Mol Vis 2006; 12:768-773. [PMID: 16862070]
    • (2006) Mol Vis , vol.12 , pp. 768-773
    • Santhiya, S.T.1    Soker, T.2    Klopp, N.3    Illig, T.4    Prakash, M.V.5    Selvaraj, B.6    Gopinath, P.M.7    Graw, J.8
  • 8
    • 33751518175 scopus 로고    scopus 로고
    • The cataractcausing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity
    • [PMID: 17149363]
    • Singh D, Raman B, Ramakrishna T, Rao Ch M. The cataractcausing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity. Mol Vis 2006; 12:1372-1379. [PMID: 17149363]
    • (2006) Mol Vis , vol.12 , pp. 1372-1379
    • Singh, D.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 9
    • 37349125494 scopus 로고    scopus 로고
    • Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity
    • [PMID: 18199971]
    • Murugesan R, Santhoshkumar P, Sharma KK. Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity. Mol Vis 2007; 13:2301-2309. [PMID: 18199971]
    • (2007) Mol Vis , vol.13 , pp. 2301-2309
    • Murugesan, R.1    Santhoshkumar, P.2    Sharma, K.K.3
  • 10
    • 11844274723 scopus 로고    scopus 로고
    • The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?
    • [PMID: 15642318]
    • Horwitz J, Huang Q, Ding L. The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function? Exp Eye Res 2004; 79:817-21. [PMID: 15642318]
    • (2004) Exp Eye Res , vol.79 , pp. 817-821
    • Horwitz, J.1    Huang, Q.2    Ding, L.3
  • 11
    • 0035853671 scopus 로고    scopus 로고
    • A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity
    • [PMID: 11278766]
    • Feil IK, Malfois M, Hendle J, van Der Zandt H, Svergun DI. A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity. J Biol Chem 2001; 276:12024-12029. [PMID: 11278766]
    • (2001) J Biol Chem , vol.276 , pp. 12024-12029
    • Feil, I.K.1    Malfois, M.2    Hendle, J.3    van Der Zandt, H.4    Svergun, D.I.5
  • 12
    • 33644690454 scopus 로고    scopus 로고
    • Mini-alphaB-crystallin: A functional element of alphaBcrystallin with chaperone-like activity
    • [PMID: 16503662]
    • Bhattacharyya J, Padmanabha Udupa EG, Wang J, Sharma KK. Mini-alphaB-crystallin: a functional element of alphaBcrystallin with chaperone-like activity. Biochemistry 2006; 45:3069-3076. [PMID: 16503662]
    • (2006) Biochemistry , vol.45 , pp. 3069-3076
    • Bhattacharyya, J.1    Padmanabha, U.E.G.2    Wang, J.3    Sharma, K.K.4
  • 13
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin
    • [PMID: 10660525]
    • Sharma KK, Kumar RS, Kumar GS, Quinn PT. Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin. J Biol Chem 2000; 275:3767-3771. [PMID: 10660525]
    • (2000) J Biol Chem , vol.275 , pp. 3767-3771
    • Sharma, K.K.1    Kumar, R.S.2    Kumar, G.S.3    Quinn, P.T.4
  • 14
    • 0034673151 scopus 로고    scopus 로고
    • Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function
    • [PMID: 10684623]
    • Shroff NP, Cherian-Shaw M, Bera S, Abraham EC. Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function. Biochemistry 2000; 39:1420-1426. [PMID: 10684623]
    • (2000) Biochemistry , vol.39 , pp. 1420-1426
    • Shroff, N.P.1    Cherian-Shaw, M.2    Bera, S.3    Abraham, E.C.4
  • 16
    • 76849101762 scopus 로고
    • Effects of congenital cataract mutation R116H on alphaA-crystallin structure, function and stability
    • [PMID: 20079887]
    • Pang M, Su JT, Feng S, Tang ZW, Gu F, Zhang M, Ma X, Yan YB. Effects of congenital cataract mutation R116H on alphaA-crystallin structure, function and stability. Biochim Biophys Acta 2010; 1804:948-956. [PMID: 20079887]
    • (1804) Biochim Biophys Acta , vol.2010 , pp. 948-956
    • Pang, M.1    Su, J.T.2    Feng, S.3    Tang, Z.W.4    Gu, F.5    Zhang, M.6    Ma, X.7    Yan, Y.B.8
  • 17
    • 0033588379 scopus 로고    scopus 로고
    • Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins
    • [PMID: 10446186]
    • Kumar LV, Ramakrishna T, Rao CM. Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins. J Biol Chem 1999; 274:24137-24141.[PMID: 10446186]
    • (1999) J Biol Chem , vol.274 , pp. 24137-24141
    • Kumar, L.V.1    Ramakrishna, T.2    Rao, C.M.3
  • 18
    • 59849129128 scopus 로고    scopus 로고
    • Abnormal assemblies and subunitexchange of alphaB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure
    • [PMID: 19140694]
    • Michiel M, Skouri-Panet F, Duprat E, Simon S, Ferard C, Tardieu A, Finet S. Abnormal assemblies and subunitexchange of alphaB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure. Biochemistry 2009; 48:442-453. [PMID: 19140694]
    • (2009) Biochemistry , vol.48 , pp. 442-453
    • Michiel, M.1    Skouri-Panet, F.2    Duprat, E.3    Simon, S.4    Ferard, C.5    Tardieu, A.6    Finet, S.7
  • 20
    • 43749091530 scopus 로고    scopus 로고
    • Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation
    • [PMID: 18227073]
    • Santhoshkumar P, Udupa P, Murugesan R, Sharma KK. Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation. J Biol Chem 2008; 283:8477-8485. [PMID: 18227073]
    • (2008) J Biol Chem , vol.283 , pp. 8477-8485
    • Santhoshkumar, P.1    Udupa, P.2    Murugesan, R.3    Sharma, K.K.4
  • 21
    • 34848908677 scopus 로고    scopus 로고
    • The role of the conserved COOH-terminal triad in alphaA-crystallin aggregation and functionality
    • [PMID: 17960114]
    • Li Y, Schmitz KR, Salerno JC, Koretz JF. The role of the conserved COOH-terminal triad in alphaA-crystallin aggregation and functionality. Mol Vis 2007; 13:1758-1768. [PMID: 17960114]
    • (2007) Mol Vis , vol.13 , pp. 1758-1768
    • Li, Y.1    Schmitz, K.R.2    Salerno, J.C.3    Koretz, J.F.4
  • 22
    • 33846050348 scopus 로고    scopus 로고
    • Role of arginine-163 and the 163REEK166 motif in the oligomerization of truncated alpha A-crystallins
    • [PMID: 17176090]
    • Rajan S, Chandrashekar R, Aziz A, Abraham EC. Role of arginine-163 and the 163REEK166 motif in the oligomerization of truncated alpha A-crystallins. Biochemistry 2006; 45:15684-15691. [PMID: 17176090]
    • (2006) Biochemistry , vol.45 , pp. 15684-15691
    • Rajan, S.1    Chandrashekar, R.2    Aziz, A.3    Abraham, E.C.4
  • 23
    • 17644408766 scopus 로고    scopus 로고
    • Subunit exchange of polydisperse proteins: Mass spectrometry reveals consequences of alphaA-crystallin truncation
    • [PMID: 15701626]
    • 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; 280:14485-14491. [PMID: 15701626]
    • (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
  • 24
    • 0028346451 scopus 로고
    • Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
    • [PMID: 8157658]
    • Kato K, Hasegawa K, Goto S, Inaguma Y. Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27. J Biol Chem 1994; 269:11274-11278. [PMID: 8157658]
    • (1994) J Biol Chem , vol.269 , pp. 11274-11278
    • Kato, K.1    Hasegawa, K.2    Goto, S.3    Inaguma, Y.4
  • 25
    • 21744448008 scopus 로고    scopus 로고
    • Structural instability caused by a mutation at a conserved arginine in the alpha-crystallin domain of Chinese hamster heat shock protein 27
    • [PMID: 16038412]
    • Chávez Zobel AT, Lambert H, Theriault JR, Landry J. Structural instability caused by a mutation at a conserved arginine in the alpha-crystallin domain of Chinese hamster heat shock protein 27. Cell Stress Chaperones 2005; 10:157-166. [PMID: 16038412]
    • (2005) Cell Stress Chaperones , vol.10 , pp. 157-166
    • Chávez, Z.A.T.1    Lambert, H.2    Theriault, J.R.3    Landry, J.4
  • 29
    • 0032530971 scopus 로고    scopus 로고
    • Identification of protein folding patterns using site-directed spin labeling. Structural characterization of a beta-sheet and putative substrate binding regions in the conserved domain of alpha A-crystallin
    • [PMID: 9737844]
    • Koteiche HA, Berengian AR, McHaourab HS. Identification of protein folding patterns using site-directed spin labeling. Structural characterization of a beta-sheet and putative substrate binding regions in the conserved domain of alpha A-crystallin. Biochemistry 1998; 37:12681-12688. [PMID: 9737844]
    • (1998) Biochemistry , vol.37 , pp. 12681-12688
    • Koteiche, H.A.1    Berengian, A.R.2    McHaourab, H.S.3
  • 31
    • 0033969150 scopus 로고    scopus 로고
    • The influence of macromolecular crowding for protein assembly
    • [PMID: 10679465]
    • Minton AP. The influence of macromolecular crowding for protein assembly. Curr Opin Struct Biol 2000; 10:34-39. [PMID: 10679465]
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 33
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins: Dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme
    • [PMID: 15542604]
    • Shashidharamurthy R, Koteiche HA, Dong J, McHaourab HS. Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme. J Biol Chem 2005; 280:5281-5289. [PMID: 15542604]
    • (2005) J Biol Chem , vol.280 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 34
    • 0037195859 scopus 로고    scopus 로고
    • Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro
    • [PMID: 12297515]
    • Giese KC, Vierling E. Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro. J Biol Chem 2002; 277:46310-46318. [PMID: 12297515]
    • (2002) J Biol Chem , vol.277 , pp. 46310-46318
    • Giese, K.C.1    Vierling, E.2
  • 35
    • 11844277108 scopus 로고    scopus 로고
    • Dissociation is not required for alphacrystallin's chaperone function
    • [PMID: 15642315]
    • Augusteyn RC. Dissociation is not required for alphacrystallin's chaperone function. Exp Eye Res 2004; 79:781-784. [PMID: 15642315]
    • (2004) Exp Eye Res , vol.79 , pp. 781-784
    • Augusteyn, R.C.1
  • 36
    • 0032546801 scopus 로고    scopus 로고
    • Identification of 1,1'-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in alpha-crystallin
    • [PMID: 9624133]
    • Sharma KK, Kumar GS, Murphy AS, Kester K. Identification of 1,1'-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in alpha-crystallin. J Biol Chem 1998; 273:15474-15478. [PMID: 9624133]
    • (1998) J Biol Chem , vol.273 , pp. 15474-15478
    • Sharma, K.K.1    Kumar, G.S.2    Murphy, A.S.3    Kester, K.4
  • 37
    • 69949088138 scopus 로고    scopus 로고
    • Degradation of proteins upon storage at near-neutral pH: Indications of a proteolytic/gelatinolytic activity associated with aggregates
    • [PMID: 19563865]
    • Sharma M, Luthra-Guptasarma M. Degradation of proteins upon storage at near-neutral pH: indications of a proteolytic/gelatinolytic activity associated with aggregates. Biochim Biophys Acta 2009; 1790:1282-1294. [PMID: 19563865]
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1282-1294
    • Sharma, M.1    Luthra-Guptasarma, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.