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Volumn 11, Issue 3, 2010, Pages 332-347

Mechanisms of function of tapasin, a critical major histocompatibility complex class i assembly factor

Author keywords

Calreticulin; ERp57; Major histocompatibility complex class I; Protein disulfide isomerase (PDI); TAP transporter; Tapasin

Indexed keywords

CALRETICULIN; ENDOPLASMIC RETICULUM PROTEIN 57; GAMMA INTERFERON; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE; TAPASIN; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING 1; UNCLASSIFIED DRUG;

EID: 77949536081     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2009.01025.x     Document Type: Article
Times cited : (32)

References (35)
  • 2
    • 0030871305 scopus 로고    scopus 로고
    • Cloning and functional characterization of a subunit of the transporter associated with antigen processing
    • Li S, Sjogren HO, Hellman U, Pettersson RF, Wang P. Cloning and functional characterization of a subunit of the transporter associated with antigen processing. Proc Natl Acad Sci U S A 1997, 94:8708-8713.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8708-8713
    • Li, S.1    Sjogren, H.O.2    Hellman, U.3    Pettersson, R.F.4    Wang, P.5
  • 4
    • 0032005348 scopus 로고    scopus 로고
    • Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line 220
    • Lehner PJ, Surman MJ, Cresswell P. Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line 220. Immunity 1998, 8:221-231.
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 5
    • 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, Hammerling GJ. A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression. Eur J Immunol 2003, 33:264-273.
    • (2003) Eur J Immunol , vol.33 , pp. 264-273
    • Garbi, N.1    Tiwari, N.2    Momburg, F.3    Hammerling, G.J.4
  • 6
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick TP, Bangia N, Peaper DR, Cresswell P. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 2002, 16:87-98.
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 7
    • 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 PA, Peaper DR, Cresswell P, Reinisch KM. Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 2009, 30:21-32.
    • (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
  • 8
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • Wearsch PA, Cresswell P. Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat Immunol 2007, 8:873-881.
    • (2007) Nat Immunol , vol.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 9
    • 48749105947 scopus 로고    scopus 로고
    • The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
    • Peaper DR, Cresswell P. The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading. Proc Natl Acad Sci U S A 2008, 105:10477-10482.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10477-10482
    • Peaper, D.R.1    Cresswell, P.2
  • 10
    • 33845327829 scopus 로고    scopus 로고
    • Direct peptide regulatable interactions between tapasin and MHC class I molecules
    • Rizvi SM, Raghavan M. Direct peptide regulatable interactions between tapasin and MHC class I molecules. Proc Natl Acad Sci 2006, 103:18220-18225.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 18220-18225
    • Rizvi, S.M.1    Raghavan, M.2
  • 11
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • Chen M, Bouvier M. Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection. EMBO J 2007, 26:1681-1690.
    • (2007) EMBO J , vol.26 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2
  • 12
    • 59449100068 scopus 로고    scopus 로고
    • Influence of the tapasin C terminus on the assembly of MHC class I allotypes
    • Simone LC, Wang X, Tuli A, McIlhaney MM, Solheim JC. Influence of the tapasin C terminus on the assembly of MHC class I allotypes. Immunogenetics 2009, 61:43-54.
    • (2009) Immunogenetics , vol.61 , pp. 43-54
    • Simone, L.C.1    Wang, X.2    Tuli, A.3    McIlhaney, M.M.4    Solheim, J.C.5
  • 13
    • 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 SR, Cho S, Ahn K. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 2006, 127:369-382.
    • (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    Ahn, K.7
  • 14
    • 56949107069 scopus 로고    scopus 로고
    • The quality control of MHC class I peptide loading
    • Wearsch PA, Cresswell P. The quality control of MHC class I peptide loading. Curr Opin Cell Biol 2008, 20:624-631.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 624-631
    • Wearsch, P.A.1    Cresswell, P.2
  • 15
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper DR, Wearsch PA, Cresswell P. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J 2005, 24:3613-3623.
    • (2005) EMBO J , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 17
    • 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 GJ, 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 2002, 168:1950-1960.
    • (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
  • 18
    • 29144466584 scopus 로고    scopus 로고
    • Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I
    • Procko E, Raghuraman G, Wiley DC, Raghavan M, Gaudet R. Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I. Immunol Cell Biol 2005, 83:475-482.
    • (2005) Immunol Cell Biol , vol.83 , pp. 475-482
    • Procko, E.1    Raghuraman, G.2    Wiley, D.C.3    Raghavan, M.4    Gaudet, R.5
  • 21
    • 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, Hammerling GJ. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat Immunol 2006, 7:93-102.
    • (2006) Nat Immunol , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 22
    • 33747766822 scopus 로고    scopus 로고
    • HLA-B44 polymorphisms at position 116 of the heavy chain influence TAP complex binding via an effect on peptide occupancy
    • Thammavongsa V, Raghuraman G, Filzen TM, Collins KL, Raghavan M. HLA-B44 polymorphisms at position 116 of the heavy chain influence TAP complex binding via an effect on peptide occupancy. J Immunol 2006, 177:3150-3161.
    • (2006) J Immunol , vol.177 , pp. 3150-3161
    • Thammavongsa, V.1    Raghuraman, G.2    Filzen, T.M.3    Collins, K.L.4    Raghavan, M.5
  • 23
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M, Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 1999, 402:90-93.
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 24
    • 70349237548 scopus 로고    scopus 로고
    • Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation
    • Vigneron N, Peaper DR, Leonhardt RM, Cresswell P. Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation. Eur J Immunol 2009, 39:2371-2376.
    • (2009) Eur J Immunol , vol.39 , pp. 2371-2376
    • Vigneron, N.1    Peaper, D.R.2    Leonhardt, R.M.3    Cresswell, P.4
  • 25
  • 27
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 2006, 124:61-73.
    • (2006) Cell , vol.124 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 28
    • 0030805217 scopus 로고    scopus 로고
    • TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin
    • Spee P, Neefjes J. TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin. Eur J Immunol 1997, 27:2441-2449.
    • (1997) Eur J Immunol , vol.27 , pp. 2441-2449
    • Spee, P.1    Neefjes, J.2
  • 29
    • 10344258588 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail
    • Roeth JF, Williams M, Kasper MR, Filzen TM, Collins KL. HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail. J Cell Biol 2004, 167:903-913.
    • (2004) J Cell Biol , vol.167 , pp. 903-913
    • Roeth, J.F.1    Williams, M.2    Kasper, M.R.3    Filzen, T.M.4    Collins, K.L.5
  • 30
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear WS, Nolan GP, Scott ML, Baltimore D. Production of high-titer helper-free retroviruses by transient transfection. Proc Natl Acad Sci U S A 1993, 90:8392-8396.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 31
    • 0033199317 scopus 로고    scopus 로고
    • Uncoupling IL-2 signals that regulate T cell proliferation, survival, and Fas-mediated activation-induced cell death
    • Van Parijs L, Refaeli Y, Lord JD, Nelson BH, Abbas AK, Baltimore D. Uncoupling IL-2 signals that regulate T cell proliferation, survival, and Fas-mediated activation-induced cell death. Immunity 1999, 11:281-288.
    • (1999) Immunity , vol.11 , pp. 281-288
    • Van Parijs, L.1    Refaeli, Y.2    Lord, J.D.3    Nelson, B.H.4    Abbas, A.K.5    Baltimore, D.6
  • 32
    • 0018500742 scopus 로고
    • Use of a monoclonal antibody (W6/32) in structural studies of HLA-A,B,C, antigens
    • Parham P, Barnstable CJ, Bodmer WF. Use of a monoclonal antibody (W6/32) in structural studies of HLA-A,B,C, antigens. J Immunol 1979, 123:342-349.
    • (1979) J Immunol , vol.123 , pp. 342-349
    • Parham, P.1    Barnstable, C.J.2    Bodmer, W.F.3
  • 33
    • 0025095531 scopus 로고
    • HLA-A- and HLA-B-specific monoclonal antibodies reactive with free heavy chains in western blots, in formalin-fixed, paraffin-embedded tissue sections and in cryo-immuno-electron microscopy
    • Stam NJ, Vroom TM, Peters PJ, Pastoors EB, Ploegh HL. HLA-A- and HLA-B-specific monoclonal antibodies reactive with free heavy chains in western blots, in formalin-fixed, paraffin-embedded tissue sections and in cryo-immuno-electron microscopy. Int Immunol 1990, 2:113-125.
    • (1990) Int Immunol , vol.2 , pp. 113-125
    • Stam, N.J.1    Vroom, T.M.2    Peters, P.J.3    Pastoors, E.B.4    Ploegh, H.L.5
  • 34
    • 0028606109 scopus 로고
    • Characteristics of peptide and major histocompatibility complex class I/beta 2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2)
    • Androlewicz MJ, Ortmann B, van Endert PM, Spies T, Cresswell P. Characteristics of peptide and major histocompatibility complex class I/beta 2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2). Proc Natl Acad Sci U S A 1994, 91:12716-12720.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12716-12720
    • Androlewicz, M.J.1    Ortmann, B.2    van Endert, P.M.3    Spies, T.4    Cresswell, P.5
  • 35
    • 0141756871 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone-specific monoclonal antibodies for flow cytometry and immunohistochemical staining
    • Ogino T, Wang X, Kato S, Miyokawa N, Harabuchi Y, Ferrone S. Endoplasmic reticulum chaperone-specific monoclonal antibodies for flow cytometry and immunohistochemical staining. Tissue Antigens 2003, 62:385-393.
    • (2003) Tissue Antigens , vol.62 , pp. 385-393
    • Ogino, T.1    Wang, X.2    Kato, S.3    Miyokawa, N.4    Harabuchi, Y.5    Ferrone, S.6


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