User menu

Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation.

Bibliographic reference Vigneron, Nathalie ; Peaper, David R ; Leonhardt, Ralf M ; Cresswell, Peter. Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation.. In: European Journal of Immunology, Vol. 39, no.9, p. 2371-2376 (2009)
Permanent URL http://hdl.handle.net/2078.1/136510
  1. Peaper David R., Cresswell Peter, Regulation of MHC Class I Assembly and Peptide Binding, 10.1146/annurev.cellbio.24.110707.175347
  2. Lehner Paul J, Surman Michael J, Cresswell Peter, Soluble Tapasin Restores MHC Class I Expression and Function in the Tapasin-Negative Cell Line .220, 10.1016/s1074-7613(00)80474-4
  3. Garbi Natalio, Tan Pamela, Diehl Alexander D., Chambers Benedict J., Ljunggren Hans-Gustaf, Momburg Frank, Hämmerling Günter J., 10.1038/79775
  4. Ortmann B., A Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes, 10.1126/science.277.5330.1306
  5. Garbi Natalio, Tiwari Neeraj, Momburg Frank, Hämmerling Günter J., A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression, 10.1002/immu.200390029
  6. Dick Tobias P, Bangia Naveen, Peaper David R, Cresswell Peter, Disulfide Bond Isomerization and the Assembly of MHC Class I-Peptide Complexes, 10.1016/s1074-7613(02)00263-7
  7. Peaper David R, Wearsch Pamela A, Cresswell Peter, Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex, 10.1038/sj.emboj.7600814
  8. Silvennoinen Laura, Myllyharju Johanna, Ruoppolo Margherita, Orrù Stefania, Caterino Marianna, Kivirikko Kari I., Koivunen Peppi, Identification and Characterization of Structural Domains of Human ERp57 : ASSOCIATION WITH CALRETICULIN REQUIRES SEVERAL DOMAINS, 10.1074/jbc.m313054200
  9. Frickel E.-M., Riek R., Jelesarov I., Helenius A., Wuthrich K., Ellgaard L., TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain, 10.1073/pnas.042699099
  10. Dong Gang, Wearsch Pamela A., Peaper David R., Cresswell Peter, Reinisch Karin M., Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer, 10.1016/j.immuni.2008.10.018
  11. Peaper D. R., Cresswell P., The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading, 10.1073/pnas.0805044105
  12. Purcell A. W., Gorman J. J., Garcia-Peydro M., Paradela A., Burrows S. R., Talbo G. H., Laham N., Peh C. A., Reynolds E. C., Lopez de Castro J. A., McCluskey J., Quantitative and Qualitative Influences of Tapasin on the Class I Peptide Repertoire, 10.4049/jimmunol.166.2.1016
  13. Williams Anthony P, Peh Chen Au, Purcell Anthony W, McCluskey James, Elliott Tim, Optimization of the MHC Class I Peptide Cargo Is Dependent on Tapasin, 10.1016/s1074-7613(02)00304-7
  14. Wearsch Pamela A, Cresswell Peter, Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer, 10.1038/ni1485
  15. Chen Mingnan, Bouvier Marlene, Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection, 10.1038/sj.emboj.7601624
  16. Petersen J. L., Hickman-Miller H. D., McIlhaney M. M., Vargas S. E., Purcell A. W., Hildebrand W. H., Solheim J. C., A Charged Amino Acid Residue in the Transmembrane/Cytoplasmic Region of Tapasin Influences MHC Class I Assembly and Maturation, 10.4049/jimmunol.174.2.962
  17. Garbi Natalio, Tanaka Satoshi, Momburg Frank, Hämmerling Günter J, Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57, 10.1038/ni1288
  18. Radcliffe Catherine M., Diedrich Gundo, Harvey David J., Dwek Raymond A., Cresswell Peter, Rudd Pauline M., Identification of Specific Glycoforms of Major Histocompatibility Complex Class I Heavy Chains Suggests That Class I Peptide Loading Is an Adaptation of the Quality Control Pathway Involving Calreticulin and ERp57, 10.1074/jbc.m202466200
  19. Trombetta Sergio E., Bosch Margarita, Parodi Armando J., Glucosylation of glycoproteins by mammalian, plant, fungal, and trypanosomatid protozoa microsomal membranes, 10.1021/bi00446a022
  20. Sousa Marcelo C., Ferrero-Garcia Miguel A., Parodi Armando J., Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase, 10.1021/bi00116a015
  21. Zernich Danielle, Purcell Anthony W., Macdonald Whitney A., Kjer-Nielsen Lars, Ely Lauren K., Laham Nihay, Crockford Tanya, Mifsud Nicole A., Bharadwaj Mandvi, Chang Linus, Tait Brian D., Holdsworth Rhonda, Brooks Andrew G., Bottomley Stephen P., Beddoe Travis, Peh Chen Au, Rossjohn Jamie, McCluskey James, Natural HLA Class I Polymorphism Controls the Pathway of Antigen Presentation and Susceptibility to Viral Evasion, 10.1084/jem.20031680
  22. Role of HLA-B*5101 binding nonamer peptides in formation of the HLA-Bw4 public epitope, 10.1093/intimm/8.7.1027
  23. Tan P., Kropshofer H., Mandelboim O., Bulbuc N., Hammerling G. J., 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, 10.4049/jimmunol.168.4.1950
  24. Leonhardt R. M., Keusekotten K., Bekpen C., Knittler M. R., Critical Role for the Tapasin-Docking Site of TAP2 in the Functional Integrity of the MHC Class I-Peptide-Loading Complex, 10.4049/jimmunol.175.8.5104
  25. Coulie P. G., Lehmann F., Lethe B., Herman J., Lurquin C., Andrawiss M., Boon T., A mutated intron sequence codes for an antigenic peptide recognized by cytolytic T lymphocytes on a human melanoma., 10.1073/pnas.92.17.7976
  26. Zhang Yinan, Kozlov Guennadi, Pocanschi Cosmin L., Brockmeier Ulf, Ireland Breanna S., Maattanen Pekka, Howe Chris, Elliott Tim, Gehring Kalle, Williams David B., 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, 10.1074/jbc.m808356200
  27. Lackman R. L., Cresswell P., Exposure of the Promonocytic Cell Line THP-1 to Escherichia coli Induces IFN- -Inducible Lysosomal Thiol Reductase Expression by Inflammatory Cytokines, 10.4049/jimmunol.177.7.4833
  28. Meyer Thomas H., van Endert Peter M., Uebel Stephan, Ehring Bettina, Tampé Robert, Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells, 10.1016/0014-5793(94)00908-2