The double role of the endoplasmic reticulum chaperone tapasin in peptide optimization of HLA class I molecules.

Abstract:

:During the assembly of the HLA class I molecules with peptides in the peptide-loading complex, a series of transient interactions are made with ER-resident chaperones. These interactions culminate in the trafficking of the HLA class I molecules to the cell surface and presentation of peptides to CD8(+) T lymphocytes. Within the peptide-loading complex, the glycoprotein tapasin exhibits a relevant function. This immunoglobulin (Ig) superfamily member in the endoplasmic reticulum membrane tethers empty HLA class I molecules to the transporter associated with antigen-processing (TAP) proteins. This review will address the current concepts regarding the double role that tapasin plays in the peptide optimization and surface expression of the HLA class I molecules.

journal_name

Scand J Immunol

authors

Cabrera CM

doi

10.1111/j.1365-3083.2007.01934.x

subject

Has Abstract

pub_date

2007-06-01 00:00:00

pages

487-93

issue

6

eissn

0300-9475

issn

1365-3083

pii

SJI1934

journal_volume

65

pub_type

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