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Volumn 21, Issue 5, 2010, Pages 512-519

ER quality control in the biogenesis of MHC class I molecules

Author keywords

Class I histocompatibility; ERp57; Molecular chaperone; Peptide loading; Tapasin; Viral evasion

Indexed keywords

CALRETICULIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEIN P57; TAPASIN; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING 1;

EID: 77952585182     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2009.12.013     Document Type: Review
Times cited : (49)

References (81)
  • 1
    • 0026022577 scopus 로고
    • Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules
    • Degen E., and Williams D.B. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. J Cell Biol 112 (1991) 1099-1115
    • (1991) J Cell Biol , vol.112 , pp. 1099-1115
    • Degen, E.1    Williams, D.B.2
  • 2
    • 26244443657 scopus 로고    scopus 로고
    • Accessory molecules in the assembly of major histocompatibility complex class I/peptide complexes: how essential are they for CD8(+) T-cell immune responses?
    • Garbi N., Tanaka S., van den Broek M., Momburg F., and Hammerling G.J. Accessory molecules in the assembly of major histocompatibility complex class I/peptide complexes: how essential are they for CD8(+) T-cell immune responses?. Immunol Rev 207 (2005) 77-88
    • (2005) Immunol Rev , vol.207 , pp. 77-88
    • Garbi, N.1    Tanaka, S.2    van den Broek, M.3    Momburg, F.4    Hammerling, G.J.5
  • 3
    • 0036776746 scopus 로고    scopus 로고
    • Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum
    • Momburg F., and Tan P. Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum. Mol Immunol 39 (2002) 217-233
    • (2002) Mol Immunol , vol.39 , pp. 217-233
    • Momburg, F.1    Tan, P.2
  • 4
    • 55849088319 scopus 로고    scopus 로고
    • Regulation of MHC class I assembly and peptide binding
    • Peaper D.R., and Cresswell P. Regulation of MHC class I assembly and peptide binding. Annu Rev Cell Dev Biol 24 (2008) 343-368
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 343-368
    • Peaper, D.R.1    Cresswell, P.2
  • 5
    • 0030765974 scopus 로고    scopus 로고
    • Beta 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins
    • Tector M., Zhang Q., and Salter R.D. Beta 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins. Mol Immunol 34 (1997) 401-408
    • (1997) Mol Immunol , vol.34 , pp. 401-408
    • Tector, M.1    Zhang, Q.2    Salter, R.D.3
  • 6
    • 33744961082 scopus 로고    scopus 로고
    • Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    • Zhang Y., Baig E., and Williams D.B. Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules. J Biol Chem 281 (2006) 14622-14631
    • (2006) J Biol Chem , vol.281 , pp. 14622-14631
    • Zhang, Y.1    Baig, E.2    Williams, D.B.3
  • 7
    • 0026740876 scopus 로고
    • Peptide-induced stabilization and intracellular localization of empty HLA class I complexes
    • Baas E.J., van Santen H.M., Kleijmeer M.J., Geuze H.J., Peters P.J., and Ploegh H.L. Peptide-induced stabilization and intracellular localization of empty HLA class I complexes. J Exp Med 176 (1992) 147-156
    • (1992) J Exp Med , vol.176 , pp. 147-156
    • Baas, E.J.1    van Santen, H.M.2    Kleijmeer, M.J.3    Geuze, H.J.4    Peters, P.J.5    Ploegh, H.L.6
  • 8
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
    • Hughes E.A., Hammond C., and Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc Natl Acad Sci USA 94 (1997) 1896-1901
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1896-1901
    • Hughes, E.A.1    Hammond, C.2    Cresswell, P.3
  • 9
    • 0028917887 scopus 로고
    • Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
    • Nossner E., and Parham P. Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules. J Exp Med 181 (1995) 327-337
    • (1995) J Exp Med , vol.181 , pp. 327-337
    • Nossner, E.1    Parham, P.2
  • 10
    • 0034799402 scopus 로고    scopus 로고
    • The Structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag J.D., Bergeron J.J., Li Y., Borisova S., Hahn M., Thomas D.Y., et al. The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol Cell 8 (2001) 633-644
    • (2001) Mol Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6
  • 12
    • 63649090633 scopus 로고    scopus 로고
    • Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function
    • Brockmeier A., Brockmeier U., and Williams D.B. Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function. J Biol Chem 284 (2009) 3433-3444
    • (2009) J Biol Chem , vol.284 , pp. 3433-3444
    • Brockmeier, A.1    Brockmeier, U.2    Williams, D.B.3
  • 13
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C., Braakman I., and Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 91 (1994) 913-917
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 14
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos A., Michalak M., Lehrman M.A., and Williams D.B. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37 (1998) 3480-3490
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 15
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa M., and Parodi A.J. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J 14 (1995) 4196-4203
    • (1995) EMBO J , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 16
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., and Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73 (2004) 1019-1049
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 17
    • 33750340637 scopus 로고    scopus 로고
    • Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum
    • Brockmeier A., and Williams D.B. Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum. Biochemistry 45 (2006) 12906-12916
    • (2006) Biochemistry , vol.45 , pp. 12906-12916
    • Brockmeier, A.1    Williams, D.B.2
  • 18
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams D.B. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 119 (2006) 615-623
    • (2006) J Cell Sci , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 19
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos A., Cohen-Doyle M.F., Peterson P.A., Jackson M.R., and Williams D.B. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J 15 (1996) 1495-1506
    • (1996) EMBO J , vol.15 , pp. 1495-1506
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 20
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson M.R., Cohen-Doyle M.F., Peterson P.A., and Williams D.B. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 263 (1994) 384-387
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 21
    • 0029552627 scopus 로고
    • Assembly, peptide loading, and transport of MHC class I molecules in a calnexin-negative cell line
    • Sadasivan B.K., Cariappa A., Waneck G.L., and Cresswell P. Assembly, peptide loading, and transport of MHC class I molecules in a calnexin-negative cell line. Cold Spring Harb Symp Quant Biol 60 (1995) 267-275
    • (1995) Cold Spring Harb Symp Quant Biol , vol.60 , pp. 267-275
    • Sadasivan, B.K.1    Cariappa, A.2    Waneck, G.L.3    Cresswell, P.4
  • 22
    • 1342334746 scopus 로고    scopus 로고
    • Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
    • Molinari M., Eriksson K.K., Calanca V., Galli C., Cresswell P., Michalak M., et al. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol Cell 13 (2004) 125-135
    • (2004) Mol Cell , vol.13 , pp. 125-135
    • Molinari, M.1    Eriksson, K.K.2    Calanca, V.3    Galli, C.4    Cresswell, P.5    Michalak, M.6
  • 23
    • 34247572423 scopus 로고    scopus 로고
    • ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove
    • Antoniou A.N., Santos S.G., Campbell E.C., Lynch S., Arosa F.A., and Powis S.J. ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove. FEBS Lett 581 (2007) 1988-1992
    • (2007) FEBS Lett , vol.581 , pp. 1988-1992
    • Antoniou, A.N.1    Santos, S.G.2    Campbell, E.C.3    Lynch, S.4    Arosa, F.A.5    Powis, S.J.6
  • 24
    • 34547092165 scopus 로고    scopus 로고
    • Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin
    • Kienast A., Preuss M., Winkler M., and Dick T.P. Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin. Nat Immunol 8 (2007) 864-872
    • (2007) Nat Immunol , vol.8 , pp. 864-872
    • Kienast, A.1    Preuss, M.2    Winkler, M.3    Dick, T.P.4
  • 25
    • 65649095933 scopus 로고    scopus 로고
    • ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity
    • Zhang Y., Kozlov G., Pocanschi C.L., Brockmeier U., Ireland B.S., Maattanen P., et al. ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity. J Biol Chem 284 (2009) 10160-10173
    • (2009) J Biol Chem , vol.284 , pp. 10160-10173
    • Zhang, Y.1    Kozlov, G.2    Pocanschi, C.L.3    Brockmeier, U.4    Ireland, B.S.5    Maattanen, P.6
  • 26
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A., Darby N.J., Tessier D.C., Michalak M., Bergeron J.J., and Thomas D.Y. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem 273 (1998) 6009-6012
    • (1998) J Biol Chem , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.5    Thomas, D.Y.6
  • 27
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M., and Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402 (1999) 90-93
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 28
    • 33746822999 scopus 로고    scopus 로고
    • Crystal structure of the bb′ domains of the protein disulfide isomerase ERp57
    • Kozlov G., Maattanen P., Schrag J.D., Pollock S., Cygler M., Nagar B., et al. Crystal structure of the bb′ domains of the protein disulfide isomerase ERp57. Structure 14 (2006) 1331-1339
    • (2006) Structure , vol.14 , pp. 1331-1339
    • Kozlov, G.1    Maattanen, P.2    Schrag, J.D.3    Pollock, S.4    Cygler, M.5    Nagar, B.6
  • 29
    • 59049105293 scopus 로고    scopus 로고
    • Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin
    • Jessop C.E., Tavender T.J., Watkins R.H., Chambers J.E., and Bulleid N.J. Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. J Biol Chem 284 (2009) 2194-2202
    • (2009) J Biol Chem , vol.284 , pp. 2194-2202
    • Jessop, C.E.1    Tavender, T.J.2    Watkins, R.H.3    Chambers, J.E.4    Bulleid, N.J.5
  • 30
    • 35548992416 scopus 로고    scopus 로고
    • Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells
    • Schelhaas M., Malmstrom J., Pelkmans L., Haugstetter J., Ellgaard L., Grunewald K., et al. Simian Virus 40 depends on ER protein folding and quality control factors for entry into host cells. Cell 131 (2007) 516-529
    • (2007) Cell , vol.131 , pp. 516-529
    • Schelhaas, M.1    Malmstrom, J.2    Pelkmans, L.3    Haugstetter, J.4    Ellgaard, L.5    Grunewald, K.6
  • 31
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick T.P., Bangia N., Peaper D.R., and Cresswell P. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 16 (2002) 87-98
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 32
    • 77952584245 scopus 로고    scopus 로고
    • A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules
    • Kang K., Park B., Oh C., Cho K., and Ahn K. A role for protein disulfide isomerase in the early folding and assembly of MHC class I molecules. Antioxid Redox Signal 11 (2009) 2553-2561
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2553-2561
    • Kang, K.1    Park, B.2    Oh, C.3    Cho, K.4    Ahn, K.5
  • 33
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper D.R., Wearsch P.A., and Cresswell P. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J 24 (2005) 3613-3623
    • (2005) EMBO J , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 34
    • 48749094772 scopus 로고    scopus 로고
    • Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
    • Ireland B.S., Brockmeier U., Howe C.M., Elliott T., and Williams D.B. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules. Mol Biol Cell 19 (2008) 2413-2423
    • (2008) Mol Biol Cell , vol.19 , pp. 2413-2423
    • Ireland, B.S.1    Brockmeier, U.2    Howe, C.M.3    Elliott, T.4    Williams, D.B.5
  • 35
    • 2942620134 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status
    • Wearsch P.A., Jakob C.A., Vallin A., Dwek R.A., Rudd P.M., and Cresswell P. Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status. J Biol Chem 279 (2004) 25112-25121
    • (2004) J Biol Chem , vol.279 , pp. 25112-25121
    • Wearsch, P.A.1    Jakob, C.A.2    Vallin, A.3    Dwek, R.A.4    Rudd, P.M.5    Cresswell, P.6
  • 36
    • 2942596020 scopus 로고    scopus 로고
    • Bap29/31 influences the intracellular traffic of MHC class I molecules
    • Paquet M.E., Cohen-Doyle M., Shore G.C., and Williams D.B. Bap29/31 influences the intracellular traffic of MHC class I molecules. J Immunol 172 (2004) 7548-7555
    • (2004) J Immunol , vol.172 , pp. 7548-7555
    • Paquet, M.E.1    Cohen-Doyle, M.2    Shore, G.C.3    Williams, D.B.4
  • 37
    • 33750320380 scopus 로고    scopus 로고
    • Bap31 enhances the endoplasmic reticulum export and quality control of human class I MHC molecules
    • Ladasky J.J., Boyle S., Seth M., Li H., Pentcheva T., Abe F., et al. Bap31 enhances the endoplasmic reticulum export and quality control of human class I MHC molecules. J Immunol 177 (2006) 6172-6181
    • (2006) J Immunol , vol.177 , pp. 6172-6181
    • Ladasky, J.J.1    Boyle, S.2    Seth, M.3    Li, H.4    Pentcheva, T.5    Abe, F.6
  • 38
    • 0025775723 scopus 로고
    • A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecules
    • Hsu V.W., Yuan L.C., Nuchtern J.G., Lippincott-Schwartz J., Hammerling G.J., and Klausner R.D. A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecules. Nature 352 (1991) 441-444
    • (1991) Nature , vol.352 , pp. 441-444
    • Hsu, V.W.1    Yuan, L.C.2    Nuchtern, J.G.3    Lippincott-Schwartz, J.4    Hammerling, G.J.5    Klausner, R.D.6
  • 40
    • 33744936808 scopus 로고    scopus 로고
    • The double lysine motif of tapasin is a retrieval signal for retention of unstable MHC class I molecules in the endoplasmic reticulum
    • Paulsson K.M., Jevon M., Wang J.W., Li S., and Wang P. The double lysine motif of tapasin is a retrieval signal for retention of unstable MHC class I molecules in the endoplasmic reticulum. J Immunol 176 (2006) 7482-7488
    • (2006) J Immunol , vol.176 , pp. 7482-7488
    • Paulsson, K.M.1    Jevon, M.2    Wang, J.W.3    Li, S.4    Wang, P.5
  • 41
    • 0037261366 scopus 로고    scopus 로고
    • A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression
    • Garbi N., Tiwari N., Momburg F., and Hammerling G.J. A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression. Eur J Immunol 33 (2003) 264-273
    • (2003) Eur J Immunol , vol.33 , pp. 264-273
    • Garbi, N.1    Tiwari, N.2    Momburg, F.3    Hammerling, G.J.4
  • 42
    • 0037083299 scopus 로고    scopus 로고
    • Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading
    • Tan P., Kropshofer H., Mandelboim O., Bulbuc N., Hammerling G.J., and Momburg F. Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading. J Immunol 168 (2002) 1950-1960
    • (2002) J Immunol , vol.168 , pp. 1950-1960
    • Tan, P.1    Kropshofer, H.2    Mandelboim, O.3    Bulbuc, N.4    Hammerling, G.J.5    Momburg, F.6
  • 43
    • 0032005348 scopus 로고    scopus 로고
    • Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220
    • Lehner P.J., Surman M.J., and Cresswell P. Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line .220. Immunity 8 (1998) 221-231
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 44
    • 0036230677 scopus 로고    scopus 로고
    • Optimization of the MHC class I peptide cargo is dependent on tapasin
    • Williams A.P., Peh C.A., Purcell A.W., McCluskey J., and Elliott T. Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 16 (2002) 509-520
    • (2002) Immunity , vol.16 , pp. 509-520
    • Williams, A.P.1    Peh, C.A.2    Purcell, A.W.3    McCluskey, J.4    Elliott, T.5
  • 45
    • 4143051423 scopus 로고    scopus 로고
    • Tapasin enhances MHC class I peptide presentation according to peptide half-life
    • Howarth M., Williams A., Tolstrup A.B., and Elliott T. Tapasin enhances MHC class I peptide presentation according to peptide half-life. Proc Natl Acad Sci USA 101 (2004) 11737-11742
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11737-11742
    • Howarth, M.1    Williams, A.2    Tolstrup, A.B.3    Elliott, T.4
  • 46
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • Chen M., and Bouvier M. Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection. EMBO J 26 (2007) 1681-1690
    • (2007) EMBO J , vol.26 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2
  • 47
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • Wearsch P.A., and Cresswell P. Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat Immunol 8 (2007) 873-881
    • (2007) Nat Immunol , vol.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 48
    • 33845327829 scopus 로고    scopus 로고
    • Direct peptide-regulatable interactions between MHC class I molecules and tapasin
    • Rizvi S.M., and Raghavan M. Direct peptide-regulatable interactions between MHC class I molecules and tapasin. Proc Natl Acad Sci USA 103 (2006) 18220-18225
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18220-18225
    • Rizvi, S.M.1    Raghavan, M.2
  • 49
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • Dong G., Wearsch P.A., Peaper D.R., Cresswell P., and Reinisch K.M. Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 30 (2009) 21-32
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 50
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • Garbi N., Tanaka S., Momburg F., and Hammerling G.J. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat Immunol 7 (2006) 93-102
    • (2006) Nat Immunol , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 51
    • 48749105947 scopus 로고    scopus 로고
    • The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
    • Peaper D.R., and Cresswell P. The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading. Proc Natl Acad Sci USA 105 (2008) 10477-10482
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10477-10482
    • Peaper, D.R.1    Cresswell, P.2
  • 52
    • 33750002010 scopus 로고    scopus 로고
    • Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing
    • Park B., Lee S., Kim E., Cho K., Riddell S.R., Cho S., et al. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127 (2006) 369-382
    • (2006) Cell , vol.127 , pp. 369-382
    • Park, B.1    Lee, S.2    Kim, E.3    Cho, K.4    Riddell, S.R.5    Cho, S.6
  • 53
    • 56949107069 scopus 로고    scopus 로고
    • The quality control of MHC class I peptide loading
    • Wearsch P.A., and Cresswell P. The quality control of MHC class I peptide loading. Curr Opin Cell Biol 20 (2008) 624-631
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 624-631
    • Wearsch, P.A.1    Cresswell, P.2
  • 54
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao B., Adhikari R., Howarth M., Nakamura K., Gold M.C., Hill A.B., et al. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16 (2002) 99-109
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3    Nakamura, K.4    Gold, M.C.5    Hill, A.B.6
  • 55
    • 77952581357 scopus 로고    scopus 로고
    • Modes of calreticulin recruitment to the major histocompatibility complex (MHC) class I assembly pathway
    • Del Cid N., Jeffery E., Rizvi S.M., Stamper E., Peters L.R., Brown W.C., et al. Modes of calreticulin recruitment to the major histocompatibility complex (MHC) class I assembly pathway. J Biol Chem December (2009)
    • (2009) J Biol Chem , Issue.December
    • Del Cid, N.1    Jeffery, E.2    Rizvi, S.M.3    Stamper, E.4    Peters, L.R.5    Brown, W.C.6
  • 56
    • 0034517368 scopus 로고    scopus 로고
    • Selective export of MHC class I molecules from the ER after their dissociation from TAP
    • Spiliotis E.T., Manley H., Osorio M., Zuniga M.C., and Edidin M. Selective export of MHC class I molecules from the ER after their dissociation from TAP. Immunity 13 (2000) 841-851
    • (2000) Immunity , vol.13 , pp. 841-851
    • Spiliotis, E.T.1    Manley, H.2    Osorio, M.3    Zuniga, M.C.4    Edidin, M.5
  • 57
    • 65249103521 scopus 로고    scopus 로고
    • Interaction of Bap31 and MHC class I molecules and their traffic out of the endoplasmic reticulum
    • Abe F., Van Prooyen N., Ladasky J.J., and Edidin M. Interaction of Bap31 and MHC class I molecules and their traffic out of the endoplasmic reticulum. J Immunol 182 (2009) 4776-4783
    • (2009) J Immunol , vol.182 , pp. 4776-4783
    • Abe, F.1    Van Prooyen, N.2    Ladasky, J.J.3    Edidin, M.4
  • 58
    • 35648938644 scopus 로고    scopus 로고
    • Peptide-receptive major histocompatibility complex class I molecules cycle between endoplasmic reticulum and cis-Golgi in wild-type lymphocytes
    • Garstka M., Borchert B., Al-Balushi M., Praveen P.V., Kuhl N., Majoul I., et al. Peptide-receptive major histocompatibility complex class I molecules cycle between endoplasmic reticulum and cis-Golgi in wild-type lymphocytes. J Biol Chem 282 (2007) 30680-30690
    • (2007) J Biol Chem , vol.282 , pp. 30680-30690
    • Garstka, M.1    Borchert, B.2    Al-Balushi, M.3    Praveen, P.V.4    Kuhl, N.5    Majoul, I.6
  • 59
    • 71349084487 scopus 로고    scopus 로고
    • Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules
    • Howe C., Garstka M., Al-Balushi M., Ghanem E., Antoniou A.N., Fritzsche S., et al. Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules. EMBO J 28 (2009) 3730-3744
    • (2009) EMBO J , vol.28 , pp. 3730-3744
    • Howe, C.1    Garstka, M.2    Al-Balushi, M.3    Ghanem, E.4    Antoniou, A.N.5    Fritzsche, S.6
  • 60
    • 0037166298 scopus 로고    scopus 로고
    • Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum
    • Paulsson K.M., Kleijmeer M.J., Griffith J., Jevon M., Chen S., Anderson P.O., et al. Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum. J Biol Chem 277 (2002) 18266-18271
    • (2002) J Biol Chem , vol.277 , pp. 18266-18271
    • Paulsson, K.M.1    Kleijmeer, M.J.2    Griffith, J.3    Jevon, M.4    Chen, S.5    Anderson, P.O.6
  • 61
    • 0026703416 scopus 로고
    • Location of MHC-encoded transporters in the endoplasmic reticulum and cis-Golgi
    • Kleijmeer M.J., Kelly A., Geuze H.J., Slot J.W., Townsend A., and Trowsdale J. Location of MHC-encoded transporters in the endoplasmic reticulum and cis-Golgi. Nature 357 (1992) 342-344
    • (1992) Nature , vol.357 , pp. 342-344
    • Kleijmeer, M.J.1    Kelly, A.2    Geuze, H.J.3    Slot, J.W.4    Townsend, A.5    Trowsdale, J.6
  • 62
    • 0035501063 scopus 로고    scopus 로고
    • Stability of surface H-2K(b), H-2D(b), and peptide-receptive H-2K(b) on splenocytes
    • Su R.C., and Miller R.G. Stability of surface H-2K(b), H-2D(b), and peptide-receptive H-2K(b) on splenocytes. J Immunol 167 (2001) 4869-4877
    • (2001) J Immunol , vol.167 , pp. 4869-4877
    • Su, R.C.1    Miller, R.G.2
  • 63
    • 0142180035 scopus 로고    scopus 로고
    • Virus evasion of MHC class I molecule presentation
    • Petersen J.L., Morris C.R., and Solheim J.C. Virus evasion of MHC class I molecule presentation. J Immunol 171 (2003) 4473-4478
    • (2003) J Immunol , vol.171 , pp. 4473-4478
    • Petersen, J.L.1    Morris, C.R.2    Solheim, J.C.3
  • 64
    • 67649842408 scopus 로고    scopus 로고
    • MHC class I antigen presentation: learning from viral evasion strategies
    • Hansen T.H., and Bouvier M. MHC class I antigen presentation: learning from viral evasion strategies. Nat Rev Immunol 9 (2009) 503-513
    • (2009) Nat Rev Immunol , vol.9 , pp. 503-513
    • Hansen, T.H.1    Bouvier, M.2
  • 65
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar S.S., and Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9 (2008) 944-957
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 66
    • 44649190782 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones participate in human cytomegalovirus US2-mediated degradation of class I major histocompatibility complex molecules
    • Oresic K., and Tortorella D. Endoplasmic reticulum chaperones participate in human cytomegalovirus US2-mediated degradation of class I major histocompatibility complex molecules. J Gen Virol 89 (2008) 1122-1130
    • (2008) J Gen Virol , vol.89 , pp. 1122-1130
    • Oresic, K.1    Tortorella, D.2
  • 67
    • 77952581545 scopus 로고    scopus 로고
    • Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation
    • Lee S.O., Cho K., Cho S., Kim I., Oh C., and Ahn K. Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation. EMBO J November (2009)
    • (2009) EMBO J , Issue.November
    • Lee, S.O.1    Cho, K.2    Cho, S.3    Kim, I.4    Oh, C.5    Ahn, K.6
  • 68
    • 65549141678 scopus 로고    scopus 로고
    • TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein
    • Oresic K., Ng C.L., and Tortorella D. TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein. J Biol Chem 284 (2009) 5905-5914
    • (2009) J Biol Chem , vol.284 , pp. 5905-5914
    • Oresic, K.1    Ng, C.L.2    Tortorella, D.3
  • 69
    • 33746370728 scopus 로고    scopus 로고
    • The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins
    • Hegde N.R., Chevalier M.S., Wisner T.W., Denton M.C., Shire K., Frappier L., et al. The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins. J Biol Chem 281 (2006) 20910-20919
    • (2006) J Biol Chem , vol.281 , pp. 20910-20919
    • Hegde, N.R.1    Chevalier, M.S.2    Wisner, T.W.3    Denton, M.C.4    Shire, K.5    Frappier, L.6
  • 70
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • Blom D., Hirsch C., Stern P., Tortorella D., and Ploegh H.L. A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J 23 (2004) 650-658
    • (2004) EMBO J , vol.23 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 71
    • 0030035445 scopus 로고    scopus 로고
    • Stable binding of the herpes simplex virus ICP47 protein to the peptide binding site of TAP
    • Tomazin R., Hill A.B., Jugovic P., York I., van Endert P., Ploegh H.L., et al. Stable binding of the herpes simplex virus ICP47 protein to the peptide binding site of TAP. EMBO J 15 (1996) 3256-3266
    • (1996) EMBO J , vol.15 , pp. 3256-3266
    • Tomazin, R.1    Hill, A.B.2    Jugovic, P.3    York, I.4    van Endert, P.5    Ploegh, H.L.6
  • 72
    • 0029034237 scopus 로고
    • Herpes simplex virus turns off the TAP to evade host immunity
    • Hill A., Jugovic P., York I., Russ G., Bennink J., Yewdell J., et al. Herpes simplex virus turns off the TAP to evade host immunity. Nature 375 (1995) 411-415
    • (1995) Nature , vol.375 , pp. 411-415
    • Hill, A.1    Jugovic, P.2    York, I.3    Russ, G.4    Bennink, J.5    Yewdell, J.6
  • 73
    • 0029069681 scopus 로고
    • A viral inhibitor of peptide transporters for antigen presentation
    • Fruh K., Ahn K., Djaballah H., Sempe P., van Endert P.M., Tampe R., et al. A viral inhibitor of peptide transporters for antigen presentation. Nature 375 (1995) 415-418
    • (1995) Nature , vol.375 , pp. 415-418
    • Fruh, K.1    Ahn, K.2    Djaballah, H.3    Sempe, P.4    van Endert, P.M.5    Tampe, R.6
  • 74
    • 0035253873 scopus 로고    scopus 로고
    • The human cytomegalovirus gene product US6 inhibits ATP binding by TAP
    • Hewitt E.W., Gupta S.S., and Lehner P.J. The human cytomegalovirus gene product US6 inhibits ATP binding by TAP. EMBO J 20 (2001) 387-396
    • (2001) EMBO J , vol.20 , pp. 387-396
    • Hewitt, E.W.1    Gupta, S.S.2    Lehner, P.J.3
  • 75
    • 1642355724 scopus 로고    scopus 로고
    • Viral degradation of the MHC class I peptide loading complex
    • Boname J.M., de Lima B.D., Lehner P.J., and Stevenson P.G. Viral degradation of the MHC class I peptide loading complex. Immunity 20 (2004) 305-317
    • (2004) Immunity , vol.20 , pp. 305-317
    • Boname, J.M.1    de Lima, B.D.2    Lehner, P.J.3    Stevenson, P.G.4
  • 76
    • 0025165899 scopus 로고
    • The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus type 2 consists of three separate amino acid segments at the carboxy terminus
    • Gabathuler R., and Kvist S. The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus type 2 consists of three separate amino acid segments at the carboxy terminus. J Cell Biol 111 (1990) 1803-1810
    • (1990) J Cell Biol , vol.111 , pp. 1803-1810
    • Gabathuler, R.1    Kvist, S.2
  • 77
    • 48249093798 scopus 로고    scopus 로고
    • Structure of UL18, a peptide-binding viral MHC mimic, bound to a host inhibitory receptor
    • Yang Z., and Bjorkman P.J. Structure of UL18, a peptide-binding viral MHC mimic, bound to a host inhibitory receptor. Proc Natl Acad Sci USA 105 (2008) 10095-10100
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10095-10100
    • Yang, Z.1    Bjorkman, P.J.2
  • 78
    • 50849088309 scopus 로고    scopus 로고
    • Human cytomegalovirus UL18 utilizes US6 for evading the NK and T-cell responses
    • Kim Y., Park B., Cho S., Shin J., Cho K., Jun Y., et al. Human cytomegalovirus UL18 utilizes US6 for evading the NK and T-cell responses. PLoS Pathog 4 (2008) e1000123
    • (2008) PLoS Pathog , vol.4
    • Kim, Y.1    Park, B.2    Cho, S.3    Shin, J.4    Cho, K.5    Jun, Y.6
  • 79
    • 26244467481 scopus 로고    scopus 로고
    • All the peptides that fit: the beginning, the middle, and the end of the MHC class I antigen-processing pathway
    • Shastri N., Cardinaud S., Schwab S.R., Serwold T., and Kunisawa J. All the peptides that fit: the beginning, the middle, and the end of the MHC class I antigen-processing pathway. Immunol Rev 207 (2005) 31-41
    • (2005) Immunol Rev , vol.207 , pp. 31-41
    • Shastri, N.1    Cardinaud, S.2    Schwab, S.R.3    Serwold, T.4    Kunisawa, J.5
  • 80
    • 70649093102 scopus 로고    scopus 로고
    • Intracellular assembly and trafficking of MHC class I molecules
    • Donaldson J.G., and Williams D.B. Intracellular assembly and trafficking of MHC class I molecules. Traffic 10 (2009) 1745-1752
    • (2009) Traffic , vol.10 , pp. 1745-1752
    • Donaldson, J.G.1    Williams, D.B.2


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