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Curr Biol. 1998 Jun 4;8(12):713-6.

A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules.

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1
MRC Protein Phosphorylation Unit, University of Dundee, Scotland.

Abstract

An important mammalian defence strategy against intracellular pathogens is the presentation of cytoplasmically derived short peptides by major histocompatibility complex (MHC) class I molecules to cytotoxic T lymphocytes. MHC class I molecules assemble in the endoplasmic reticulum (ER) with chaperones, including calnexin and calreticulin, before binding to the transporter associated with antigen processing (TAP). We show here that the thiol-dependent reductase ERp57 (also known as ER60 protease) is involved in MHC class I assembly. ERp57 co-purified with the rat TAP complex (comprising TAP1 and TAP2), and associated with MHC class I molecules at an early stage in their biosynthesis. This association was sensitive to castanospermine, which inhibits the processing of glycoproteins. Human MHC class I molecules were also found to associate with ERp57. We conclude that ERp57 is a newly identified component of the MHC class I pathway, and that it appears to interact with MHC class I molecules before they associate with TAP.

PMID:
9637924
DOI:
10.1016/s0960-9822(98)70279-9
[Indexed for MEDLINE]
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