description
Unlike other glycoproteins, correct folding of MHC class I molecules is not sufficient to trigger their exit from the ER, they exit only after peptide loading. Described here is the process of antigen presentation which consists of the folding, assembly, and peptide loading of MHC class I molecules. The newly synthesized MHC class I Heavy Chain (HC) is initially folded with the help of several chaperones (calnexin, BiP, ERp57) and then binds with Beta-2-microglobulin (B2M). This MHC:B2M heterodimer enters the peptide loading complex (PLC), a multiprotein complex that includes calreticulin, endoplasmic reticulum resident protein 57 (ERp57), transporter associated with antigen processing (TAP) and tapasin. Peptides generated from Ub-proteolysis are transported into the ER through TAP. These peptides are further trimmed by ER-associated aminopeptidase (ERAP) and loaded on to MHC class I molecules. Stable MHC class I trimers with high-affinity peptide are transported from the ER to the cell surface by the Golgi apparatus

external resources
NCBI:1269194
REACTOME:R-HSA-983170
PUBMED:19178136
PUBMED:18926908
PUBMED:12495737
PUBMED:15224092
PUBMED:18641646

genes
B2M , CALR , CANX , PDIA3 , HLA-A , HLA-B , HLA-C , HLA-E , HLA-F , HLA-G , HLA-H , HSPA5 , SEC13 , TAP1 , TAP2 , TAPBP , SEC24C , SEC24D , SEC24B , SEC23A , SEC24A , SEC31A , SAR1B , ERAP1 , ERAP2 ,