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

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Vigneron, Nathalie [UCL] Peaper, David R Leonhardt, Ralf M Cresswell, Peter

Tapasin is disulfide linked to ERp57 within the peptide loading complex. In cell-free assays, a soluble variant of the tapasin/ERp57 dimer recruits MHC class I molecules and promotes peptide binding to them, whereas soluble tapasin alone does not. Here we show that within cells, tapasin conjugation with ERp57 is as critical as its integration into the membrane for efficient MHC class I assembly, surface expression, and Ag presentation to CD8(+) T cells. Elimination of both of these properties severely compromises tapasin function, in keeping with predictions from in vitro studies.

Document type Article de périodique (Journal article)
Access type Accès restreint
Publication date 2009
Language Anglais
Journal information "European Journal of Immunology" - Vol. 39, no.9, p. 2371-2376 (2009)
Peer reviewed yes
Publisher Wiley - V C H Verlag GmbH & Co. KGaA ((Germany) Weinheim)
issn 0014-2980
e-issn 1521-4141
Publication status Publié
Affiliation UCL - SSS/DDUV - Institut de Duve
MESH Subject Antigen Presentation ; Cell Line ; Cell Membrane ; Histocompatibility Antigens Class I ; Humans ; Membrane Transport Proteins ; Protein Binding ; Protein Disulfide-Isomerases ; T-Lymphocytes, Cytotoxic
Links
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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