메뉴 건너뛰기




Volumn 46, Issue 10, 2009, Pages 2147-2150

A transmembrane tail: Interaction of tapasin with TAP and the MHC class I molecule

Author keywords

Antigen presentation processing; Major histocompatibility complex; Tapasin; Transmembrane; Transporter associated with antigen processing

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; TAPASIN;

EID: 67349111344     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2009.03.006     Document Type: Article
Times cited : (4)

References (25)
  • 1
    • 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., Solheim J.C., Harris M., Stroynowski I., Connolly J.M., and Hansen T.H. TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J. Immunol. 155 (1995) 4726-4733
    • (1995) J. Immunol. , vol.155 , pp. 4726-4733
    • Carreno, B.M.1    Solheim, J.C.2    Harris, M.3    Stroynowski, I.4    Connolly, J.M.5    Hansen, T.H.6
  • 2
    • 38349107628 scopus 로고    scopus 로고
    • Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly
    • Chambers J.E., Jessop C.E., and Bulleid N.J. Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly. J. Biol. Chem. 283 (2008) 1862-1869
    • (2008) J. Biol. Chem. , vol.283 , pp. 1862-1869
    • Chambers, J.E.1    Jessop, C.E.2    Bulleid, N.J.3
  • 4
    • 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
  • 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., 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
  • 6
    • 33846044754 scopus 로고    scopus 로고
    • Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes
    • Garbi N., Hammerling G., and Tanaka S. Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes. Curr. Opin. Immunol. 19 (2007) 99-105
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 99-105
    • Garbi, N.1    Hammerling, G.2    Tanaka, S.3
  • 8
    • 1642290656 scopus 로고    scopus 로고
    • Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP)
    • Koch J., Guntrum R., Heintke S., Kyritsis C., and Tampe R. Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP). J. Biol. Chem. 279 (2004) 10142-10147
    • (2004) J. Biol. Chem. , vol.279 , pp. 10142-10147
    • Koch, J.1    Guntrum, R.2    Heintke, S.3    Kyritsis, C.4    Tampe, R.5
  • 9
    • 33745848754 scopus 로고    scopus 로고
    • The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin binding
    • Koch J., Guntrum R., and Tampe R. The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin binding. FEBS Lett. 580 (2006) 4091-4096
    • (2006) FEBS Lett. , vol.580 , pp. 4091-4096
    • Koch, J.1    Guntrum, R.2    Tampe, R.3
  • 10
    • 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
  • 11
    • 26844477450 scopus 로고    scopus 로고
    • Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex
    • Leonhardt R.M., Keusekotten K., Bekpen C., and Knittler M.R. Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex. J. Immunol. 175 (2005) 5104-5114
    • (2005) J. Immunol. , vol.175 , pp. 5104-5114
    • Leonhardt, R.M.1    Keusekotten, K.2    Bekpen, C.3    Knittler, M.R.4
  • 12
    • 0037372352 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints
    • Marassi F.M., and Opella S.J. Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci. 12 (2003) 403-411
    • (2003) Protein Sci. , vol.12 , pp. 403-411
    • Marassi, F.M.1    Opella, S.J.2
  • 14
    • 34248208652 scopus 로고    scopus 로고
    • Multiple residues in the transmembrane helix and connecting peptide of mouse tapasin stabilize the transporter associated with the antigen-processing TAP2 subunit
    • Papadopoulos M., and Momburg F. Multiple residues in the transmembrane helix and connecting peptide of mouse tapasin stabilize the transporter associated with the antigen-processing TAP2 subunit. J. Biol. Chem. 282 (2007) 9401-9410
    • (2007) J. Biol. Chem. , vol.282 , pp. 9401-9410
    • Papadopoulos, M.1    Momburg, F.2
  • 16
    • 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 D.C., Raghavan M., and 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. 83 (2005) 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
  • 18
    • 0036829793 scopus 로고    scopus 로고
    • Tapasin interacts with the membrane-spanning domains of both TAP subunits and enhances the structural stability of TAP1 × TAP2 complexes
    • Raghuraman G., Lapinski P.E., and Raghavan M. Tapasin interacts with the membrane-spanning domains of both TAP subunits and enhances the structural stability of TAP1 × TAP2 complexes. J. Biol. Chem. 277 (2002) 41786-41794
    • (2002) J. Biol. Chem. , vol.277 , pp. 41786-41794
    • Raghuraman, G.1    Lapinski, P.E.2    Raghavan, M.3
  • 19
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan B., Lehner P.J., Ortmann B., Spies T., and Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5 (1996) 103-114
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 20
    • 59449100068 scopus 로고    scopus 로고
    • Influence of the tapasin C terminus on the assembly of MHC class I allotypes
    • Simone L.C., Wang X., Tuli A., McIlhaney M.M., and Solheim J.C. Influence of the tapasin C terminus on the assembly of MHC class I allotypes. Immunogenetics 61 (2009) 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
  • 21
    • 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., Mitchell E.K., Yang Y., Peterson P.A., Waneck G.L., and Williams D.B. 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 (1996) 337-348
    • (1996) J. Exp. Med. , vol.184 , pp. 337-348
    • Suh, W.K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.A.4    Waneck, G.L.5    Williams, D.B.6
  • 22
    • 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
  • 23
    • 0036235698 scopus 로고    scopus 로고
    • The interface between tapasin and MHC class I: identification of amino acid residues in both proteins that influence their interaction
    • Turnquist H.R., Vargas S.E., Schenk E.L., McIlhaney M.M., Reber A.J., and Solheim J.C. The interface between tapasin and MHC class I: identification of amino acid residues in both proteins that influence their interaction. Immunol. Res. 25 (2002) 261-269
    • (2002) Immunol. Res. , vol.25 , pp. 261-269
    • Turnquist, H.R.1    Vargas, S.E.2    Schenk, E.L.3    McIlhaney, M.M.4    Reber, A.J.5    Solheim, J.C.6
  • 24
    • 16344390562 scopus 로고    scopus 로고
    • Properties of integral membrane protein structures: derivation of an implicit membrane potential
    • Ulmschneider M.B., Sansom M.S., and Di Nola A. Properties of integral membrane protein structures: derivation of an implicit membrane potential. Proteins 59 (2005) 252-265
    • (2005) Proteins , vol.59 , pp. 252-265
    • Ulmschneider, M.B.1    Sansom, M.S.2    Di Nola, A.3
  • 25
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.