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
dc.contributor.author | Procko, Erik | |
dc.contributor.author | Raghuraman, Gayatri | |
dc.contributor.author | Wiley, Don C | |
dc.contributor.author | Raghavan, Malini | |
dc.contributor.author | Gaudet, Rachelle | |
dc.date.accessioned | 2018-02-05T16:38:35Z | |
dc.date.available | 2018-02-05T16:38:35Z | |
dc.date.issued | 2005-10 | |
dc.identifier.citation | Procko, Erik; Raghuraman, Gayatri; Wiley, Don C; Raghavan, Malini; Gaudet, Rachelle (2005). "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." Immunology and Cell Biology 83(5): 475-482. | |
dc.identifier.issn | 0818-9641 | |
dc.identifier.issn | 1440-1711 | |
dc.identifier.uri | https://hdl.handle.net/2027.42/141680 | |
dc.publisher | Nature Publishing Group | |
dc.publisher | Wiley Periodicals, Inc. | |
dc.subject.other | transporter associated with antigen processing (TAP) | |
dc.subject.other | tapasin | |
dc.subject.other | antigen presentation | |
dc.subject.other | ATP‐binding cassette (ABC) transporter | |
dc.title | 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 | |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | |
dc.subject.hlbsecondlevel | Microbiology and Immunology | |
dc.subject.hlbtoplevel | Health Sciences | |
dc.description.peerreviewed | Peer Reviewed | |
dc.description.bitstreamurl | https://deepblue.lib.umich.edu/bitstream/2027.42/141680/1/imcb200564.pdf | |
dc.identifier.doi | 10.1111/j.1440-1711.2005.01354.x | |
dc.identifier.source | Immunology and Cell Biology | |
dc.identifier.citedreference | Nijenhuis M, Hammerling GJ. Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site. J. Immunol. 1996; 157: 5467 – 77. | |
dc.identifier.citedreference | Ortmann B, Androlewicz MJ, Cresswell P. MHC class I/beta 2‐microglobulin complexes associate with TAP transporters before peptide binding. Nature 1994; 368: 864 – 7. | |
dc.identifier.citedreference | Raghuraman G, Lapinski PE, Raghavan M. Tapasin interacts with the membrane‐spanning domains of both TAP subunits and enhances the structural stability of TAP1 x TAP2 complexes. J. Biol. Chem. 2002; 277: 41 786 – 94. | |
dc.identifier.citedreference | 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 – 73. | |
dc.identifier.citedreference | Nijenhuis M, Schmitt S, Armandola EA, Obst R, Brunner J, Hammerling GJ. Identification of a contact region for peptide on the TAP1 chain of the transporter associated with antigen processing. J. Immunol. 1996; 156: 2186 – 95. | |
dc.identifier.citedreference | 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. USA 1994; 91: 12 716 – 20. | |
dc.identifier.citedreference | Sadasivan B, Lehner PJ, Ortmann B, Spies T, Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 1996; 5: 103 – 14. | |
dc.identifier.citedreference | 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 – 25. | |
dc.identifier.citedreference | Ortmann B, Copeman J, Lehner PJ et al. A critical role for tapasin in the assembly and function of multimeric MHC class I‐TAP complexes. Science 1997; 277: 1306 – 309. | |
dc.identifier.citedreference | Lapinski PE, Neubig RR, Raghavan M, Walker A. Lysine mutations of TAP1 and TAP2 interfere with peptide translocation but not peptide binding. J. Biol. Chem. 2001; 276: 7526 – 33. | |
dc.identifier.citedreference | Neumann L, Tampe R. Kinetic analysis of peptide binding to the TAP transport complex: evidence for structural rearrangements induced by substrate binding. J. Mol. Biol. 1999; 294: 1203 – 13. | |
dc.identifier.citedreference | Lauvau G, Gubler B, Cohen H, Daniel S, Caillat‐Zucman S, van Endert PM. Tapasin enhances assembly of transporters associated with antigen processing‐dependent and ‐independent peptides with HLA‐A2 and HLA‐B27 expressed in insect cells. J. Biol. Chem. 1999; 274: 31 349 – 58. | |
dc.identifier.citedreference | Peh CA, Burrows SR, Barnden M et al. HLA‐B27‐restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 1998; 8: 531 – 42. | |
dc.identifier.citedreference | Muller KM, Ebensperger C, Tampe R. Nucleotide binding to the hydrophilic C‐terminal domain of the transporter associated with antigen processing (TAP). J. Biol. Chem. 1994; 269: 14 032 – 7. | |
dc.identifier.citedreference | 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 – 31. | |
dc.identifier.citedreference | Paulsson KM, Anderson PO, Chen S et al. Assembly of tapasin‐associated MHC class I in the absence of the transporter associated with antigen processing (TAP). Int. Immunol. 2001; 13: 23 – 9. | |
dc.identifier.citedreference | 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 – 60. | |
dc.identifier.citedreference | Antoniou AN, Ford S, Pilley ES, Blake N, Powis SJ. Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits. Immunology 2002; 106: 182 – 9. | |
dc.identifier.citedreference | Chang G, Roth CB. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 2001; 293: 1793 – 800. | |
dc.identifier.citedreference | Chang G. Structure of MsbA from Vibrio cholera: a multidrug resistance ABC transporter homolog in a closed conformation. J. Mol. Biol. 2003; 330: 419 – 30. | |
dc.identifier.citedreference | Bangia N, Cresswell P. Stoichiometric tapasin interactions in the catalysis of major histocompatibility complex class I molecule assembly. Immunology 2005; 114: 346 – 53. | |
dc.identifier.citedreference | Knittler MR, Alberts P, Deverson EV, Howard JC. Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules. Curr. Biol. 1999; 9: 999 – 1008. | |
dc.identifier.citedreference | Higgins CF. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 1992; 8: 67 – 113. | |
dc.identifier.citedreference | Nikaido H, Hall JA. Overview of bacterial ABC transporters. Methods Enzymol. 1998; 292: 3 – 20. | |
dc.identifier.citedreference | van Endert PM, Saveanu L, Hewitt EW, Lehner P. Powering the peptide pump: TAP crosstalk with energetic nucleotides. Trends Biochem. Sci. 2002; 27: 454 – 61. | |
dc.identifier.citedreference | Vos JC, Spee P, Momburg F, Neefjes J. Membrane topology and dimerization of the two subunits of the transporter associated with antigen processing reveal a three‐domain structure. J. Immunol. 1999; 163: 6679 – 85. | |
dc.identifier.citedreference | Vos JC, Reits EA, Wojcik‐Jacobs E, Neefjes J. Head‐head/tail‐tail relative orientation of the pore‐forming domains of the heterodimeric ABC transporter TAP. Curr. Biol. 2000; 10: 1 – 7. | |
dc.identifier.citedreference | Koch J, Guntrum R, Heintke S, Kyritsis C, Tampe R. Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP). J. Biol. Chem. 2004; 279: 10 142 – 7. | |
dc.identifier.citedreference | Bangia N, Lehner PJ, Hughes EA, Surman M, Cresswell P. The N‐terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur. J. Immunol. 1999; 29: 1858 – 70. | |
dc.identifier.citedreference | Momburg F, Tan P. Tapasin – the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum. Mol. Immunol. 2002; 39: 217 – 33. | |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.