메뉴 건너뛰기




Volumn 160, Issue 2, 1998, Pages 831-837

Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; BETA 2 MICROGLOBULIN; CALNEXIN; CALRETICULIN; CHAPERONE; GLYCAN; LECTIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MUTANT PROTEIN;

EID: 0031963654     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (47)

References (35)
  • 1
    • 0026022577 scopus 로고
    • Participation of a novel 88 kd protein in the biogenesis of murine class I histocompatibility molecules
    • Degen, E., and D. B. Williams. 1991. Participation of a novel 88 kd protein in the biogenesis of murine class I histocompatibility molecules. J. Cell Biol. 112:1099.
    • (1991) J. Cell Biol. , vol.112 , pp. 1099
    • Degen, E.1    Williams, D.B.2
  • 2
    • 0027156495 scopus 로고
    • Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)
    • David, V., F. Hochstenbach, S. Rajagapolan, and M. B. Brenner. 1993. Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J. Biol. Chem. 268:9585.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9585
    • David, V.1    Hochstenbach, F.2    Rajagapolan, S.3    Brenner, M.B.4
  • 4
    • 0028221225 scopus 로고
    • Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum
    • Rajagopalan, S., and M. B. Brenner. 1994. Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum. J. Exp. Med. 180:407.
    • (1994) J. Exp. Med. , vol.180 , pp. 407
    • Rajagopalan, S.1    Brenner, M.B.2
  • 5
    • 0028170597 scopus 로고
    • 2-microglobulin: Major histocompatibility complex class 1 heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide
    • 2-microglobulin: major histocompatibility complex class 1 heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide. J. Exp. Med. 180:2163.
    • (1994) J. Exp. Med. , vol.180 , pp. 2163
    • Sugita, M.1    Brenner, M.B.2
  • 6
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, 1P90)
    • Jackson, M. R., M. F. Cohen-Doyle, P. Peterson, and D. B. Williams. 1994. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, 1P90). Science 263:384.
    • (1994) Science , vol.263 , pp. 384
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.3    Williams, D.B.4
  • 7
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds glc1 man9glcnac2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware, F. E., A. Vassilakos, P. A. Peterson, M. R. Jackson, M. A. Lehrman, and D. B.Williams. 1995. The molecular chaperone calnexin binds glc1 man9glcnac2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 270:4697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4697
    • Ware, F.E.1    Vassilakos, A.2    Peterson, P.A.3    Jackson, M.R.4    Lehrman, M.A.5    Williams, D.B.6
  • 8
    • 0028906481 scopus 로고
    • Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules
    • Zhang, Q., M. Tector, and R. D. Salter. 1995. Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules. J. Biol. Chem. 270:3944.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3944
    • Zhang, Q.1    Tector, M.2    Salter, R.D.3
  • 9
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos, A., M. F. Cohen-Doyle, P. Peterson, M. R. Jackson, and D. B. Williams. 1996. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15:1495.
    • (1996) EMBO J. , vol.15 , pp. 1495
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.3    Jackson, M.R.4    Williams, D.B.5
  • 10
    • 0029813510 scopus 로고    scopus 로고
    • MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains
    • Suh, W.-K., E. K. Mitchell, Y. Yang, P. Peterson, G. L. Waneck, and D. B. Williams. 1996. MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J. Exp. Med. 184:337.
    • (1996) J. Exp. Med. , vol.184 , pp. 337
    • Suh, W.-K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.4    Waneck, G.L.5    Williams, D.B.6
  • 11
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I proteins with TAP
    • Sadasivan, B. K., P. J. Lehner, B. Ortmann, T. Spies, and P. Cresswell. 1996. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I proteins with TAP. Immunity 5:103.
    • (1996) Immunity , vol.5 , pp. 103
    • Sadasivan, B.K.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 12
    • 0031091739 scopus 로고    scopus 로고
    • 2-microglobulin, class 1 heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing
    • 2-microglobulin, class 1 heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing. J. Immunol. 158:2236.
    • (1997) J. Immunol. , vol.158 , pp. 2236
    • Solheim, J.C.1    Harris, M.R.2    Kindle, C.S.3    Hansen, T.H.4
  • 13
    • 0028858641 scopus 로고
    • TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man
    • Carreno, B. M., J. C. Solheim, M. Harris, I. Stroynowski, J. M. Connolly, and T. H. Hansen. 1995. TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J. Immunol. 155:4726.
    • (1995) J. Immunol. , vol.155 , pp. 4726
    • Carreno, B.M.1    Solheim, J.C.2    Harris, M.3    Stroynowski, I.4    Connolly, J.M.5    Hansen, T.H.6
  • 14
    • 0028282108 scopus 로고
    • 2-microglobulin complexes associate with TAP transporters before peptide binding
    • 2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 368:864.
    • (1994) Nature , vol.368 , pp. 864
    • Ortmann, B.1    Androlewicz, M.J.2    Cresswell, P.3
  • 16
    • 0028917887 scopus 로고
    • Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
    • Nossner, E., and P. Parham. 1995. Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules. J. Exp. Med. 181:327.
    • (1995) J. Exp. Med. , vol.181 , pp. 327
    • Nossner, E.1    Parham, P.2
  • 17
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., I. Braakman, and A. Helenius. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91:913.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 18
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BIP and calnexin
    • Hammond, C., and A. Helenius. 1994. Folding of VSV G protein: sequential interaction with BIP and calnexin. Science 266:456.
    • (1994) Science , vol.266 , pp. 456
    • Hammond, C.1    Helenius, A.2
  • 19
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D. N., B. Foellmer, and A. Helenius. 1996. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15:2961.
    • (1996) EMBO J. , vol.15 , pp. 2961
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 20
    • 0029160540 scopus 로고
    • Transient lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson, J. R., A. Ora, P. Van Nguyen, and A. Helenius. 1995. Transient lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol Biol. Cell 6:1173.
    • (1995) Mol Biol. Cell , vol.6 , pp. 1173
    • Peterson, J.R.1    Ora, A.2    Van Nguyen, P.3    Helenius, A.4
  • 21
    • 0030933129 scopus 로고    scopus 로고
    • Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
    • Zapun, A., S. F. Petrescu, P. M. Rudd, R. A. Dwek, D. Y. Thomas, and J. J. M. Bergeron. 1997. Conformation-independent binding of monoglucosylated ribonuclease B to calnexin. Cell 88:29.
    • (1997) Cell , vol.88 , pp. 29
    • Zapun, A.1    Petrescu, S.F.2    Rudd, P.M.3    Dwek, R.A.4    Thomas, D.Y.5    Bergeron, J.J.M.6
  • 22
    • 0023233777 scopus 로고
    • Comparison of the primary structure of class 1 molecules
    • Maloy, W. L. 1987. Comparison of the primary structure of class 1 molecules. Immunol. Res. 6:11.
    • (1987) Immunol. Res. , vol.6 , pp. 11
    • Maloy, W.L.1
  • 23
    • 0026521967 scopus 로고
    • The HLA-B "negative" mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon
    • Zemmour, J., A.-M. Little, D. J. Schendel, and P. Parham. 1992. The HLA-B "negative" mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon. J. Immunol. 148:1941.
    • (1992) J. Immunol. , vol.148 , pp. 1941
    • Zemmour, J.1    Little, A.-M.2    Schendel, D.J.3    Parham, P.4
  • 24
    • 0020674889 scopus 로고
    • 2-microglobulin in Daudi cells: Active gene but inactive messenger RNA
    • 2-microglobulin in Daudi cells: active gene but inactive messenger RNA. Immunogenetics 17:133.
    • (1983) Immunogenetics , vol.17 , pp. 133
    • De Preval, C.1    Mach, B.2
  • 25
    • 0018500742 scopus 로고
    • Use of monoclonal antibody (W6/32) in structural studies of HLA-A,B,C antigens
    • Parham, P., C. J. Barnstable, and W. F. Bodmer. 1979. Use of monoclonal antibody (W6/32) in structural studies of HLA-A,B,C antigens. J. Immunol. 123: 342.
    • (1979) J. Immunol. , vol.123 , pp. 342
    • Parham, P.1    Barnstable, C.J.2    Bodmer, W.F.3
  • 26
    • 0019806243 scopus 로고
    • Partial purification and some properties of BB7.2: A cytotoxic monoclonal antibody with specificity for HLA-A2 and a variant of HLA-A28
    • Parham, P., and F. M. Brodsky. 1981. Partial purification and some properties of BB7.2: a cytotoxic monoclonal antibody with specificity for HLA-A2 and a variant of HLA-A28. Hum. Immunol. 3:277.
    • (1981) Hum. Immunol. , vol.3 , pp. 277
    • Parham, P.1    Brodsky, F.M.2
  • 27
    • 0026509280 scopus 로고
    • Assembly and transport properties of invariant chain trimers and HLA-DR-invariant chain complexes
    • Lamb, C. A., and P. Cresswell. 1992. Assembly and transport properties of invariant chain trimers and HLA-DR-invariant chain complexes. J. Immunol. 148: 3478.
    • (1992) J. Immunol. , vol.148 , pp. 3478
    • Lamb, C.A.1    Cresswell, P.2
  • 28
    • 0026511275 scopus 로고
    • Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
    • Hochstenbach, F., V. David, S. Watkins, and M. B. Brenner. 1992. Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Natl. Acad. Sci. USA 89:4734.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4734
    • Hochstenbach, F.1    David, V.2    Watkins, S.3    Brenner, M.B.4
  • 30
    • 2642699794 scopus 로고    scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488.
    • Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488
    • Kunkel, T.A.1
  • 31
    • 0029073719 scopus 로고
    • Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin: Evidence implicating the class I-connecting peptide segment in calnexin association
    • Carreno, B. M., K. L. Schreiber, D. J. McKean, I. Stroynowski, and T. H. Hansen. 1995. Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin: evidence implicating the class I-connecting peptide segment in calnexin association. J. Immunol. 154:5173.
    • (1995) J. Immunol. , vol.154 , pp. 5173
    • Carreno, B.M.1    Schreiber, K.L.2    McKean, D.J.3    Stroynowski, I.4    Hansen, T.H.5
  • 32
    • 0028888054 scopus 로고
    • Molecular requirements for the interaction of class II major histocompatibility complex molecules and invariant chain with calnexin
    • Arunachalam, B., and P. Cresswell. 1995. Molecular requirements for the interaction of class II major histocompatibility complex molecules and invariant chain with calnexin. J. Biol. Chem. 270:2784.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2784
    • Arunachalam, B.1    Cresswell, P.2
  • 33
    • 0028859532 scopus 로고
    • Inhibition of invariant chain (Ii)-calnexin interaction results in enhanced degradation of Ii but does not prevent the assembly of alpha beta Ii complexes
    • Romagnoli, P., and R. N. Germain. 1995. Inhibition of invariant chain (Ii)-calnexin interaction results in enhanced degradation of Ii but does not prevent the assembly of alpha beta Ii complexes. J. Exp. Med. 182:2027.
    • (1995) J. Exp. Med. , vol.182 , pp. 2027
    • Romagnoli, P.1    Germain, R.N.2
  • 34
    • 0030765974 scopus 로고    scopus 로고
    • 2-Microglobulin and calnexin can independently promote folding and disulfide bond formation of class 1 histocompatibilily proteins
    • 2-Microglobulin and calnexin can independently promote folding and disulfide bond formation of class 1 histocompatibilily proteins. Mol. Immunol. 34:401.
    • (1997) Mol. Immunol. , vol.34 , pp. 401
    • Tector, M.1    Zhang, Q.2    Salter, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.