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Major histocompatibility complex class I antigen presentation

Major histocompatibility complex class I antigen presentation
Major histocompatibility complex class I antigen presentation
At the cell surface the function of Major Histocompatibility Complex class I proteins (MHC I) is to present peptide to T cell receptors (TcR) and recruit cofactor CD8. Inside the cell the function of MHC I is to select peptides for presentation (collectively forming the immunome) from a pool (collectively called the peptidome) derived mainly in the cytoplasm and delivered to the endoplasmic reticulum by TAP, the transporter associated with antigen presentation. MHC I peptide selection is assisted by cofactors in the early secretory pathway including the peptide-loading complex (PLC) in the ER which comprises newly assembled MHCI:beta2-microglobulin (b2m), tapasin, ERp57, calreticulin and TAP; and UDP-glucose:glycoprotein glucosyltransferase (UGGT), the tapasin-related protein TAPBPR and calreticulin in the Cis-Golgi. Initial binding of peptides to MHC is not thought to be very selective: selection is achieved by subsequent “filtration” or “refinement” steps. The first occurs in the PLC and is assisted primarily by tapasin; the second occurs in the cis Golgi network and is assisted primarily by TAPBPR, UGGT and calreticulin, and the third occurs at the cell surface.
Academic Press
Van Hateren, Andrew
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Ratcliffe, Michael
Van Hateren, Andrew
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Ratcliffe, Michael

Van Hateren, Andrew (2016) Major histocompatibility complex class I antigen presentation. In, Ratcliffe, Michael (ed.) Encyclopedia of Immunobiology. 1 ed. Academic Press.

Record type: Book Section

Abstract

At the cell surface the function of Major Histocompatibility Complex class I proteins (MHC I) is to present peptide to T cell receptors (TcR) and recruit cofactor CD8. Inside the cell the function of MHC I is to select peptides for presentation (collectively forming the immunome) from a pool (collectively called the peptidome) derived mainly in the cytoplasm and delivered to the endoplasmic reticulum by TAP, the transporter associated with antigen presentation. MHC I peptide selection is assisted by cofactors in the early secretory pathway including the peptide-loading complex (PLC) in the ER which comprises newly assembled MHCI:beta2-microglobulin (b2m), tapasin, ERp57, calreticulin and TAP; and UDP-glucose:glycoprotein glucosyltransferase (UGGT), the tapasin-related protein TAPBPR and calreticulin in the Cis-Golgi. Initial binding of peptides to MHC is not thought to be very selective: selection is achieved by subsequent “filtration” or “refinement” steps. The first occurs in the PLC and is assisted primarily by tapasin; the second occurs in the cis Golgi network and is assisted primarily by TAPBPR, UGGT and calreticulin, and the third occurs at the cell surface.

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Published date: 27 April 2016

Identifiers

Local EPrints ID: 417906
URI: http://eprints.soton.ac.uk/id/eprint/417906
PURE UUID: 69bb00ec-0a17-40c1-be91-8be1580d5e84
ORCID for Andrew Van Hateren: ORCID iD orcid.org/0000-0002-3915-0239

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Date deposited: 16 Feb 2018 17:30
Last modified: 06 Jan 2023 02:41

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Editor: Michael Ratcliffe

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