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TAP Peptide Transporters and Antigen Presentation

  • Chapter
MHC Molecules: Expression, Assembly and Function

Abstract

Since the pioneering work of Townsend and colleagues we know that class I molecules of the major histocompatibility complex (MHC) present antigenic peptides at the cell surface mostly originating from endogenously synthesized proteins that have no access to the secretory compartment.1–3 Following their formation through the activity of cytosolic proteases, such peptide epitopes need to be transported across the membrane of the endoplasmic reticulum (ER) in order to associate with the peptide binding groove of newly synthesized class I molecules. This topological problem prompted the search for a cell-biological mechanism mediating vectorial peptide transport into the ER. Five years ago, genetic approaches provided a satisfying explanation with the discovery of putative transporter molecules in the ER membrane that are now called TAP (“transporters associated with antigen processing”).

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Momburg, F., Hämmerling, G.J., Neefjes, J.J. (1996). TAP Peptide Transporters and Antigen Presentation. In: MHC Molecules: Expression, Assembly and Function. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6462-7_3

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