Chaperone function in antigen presentation by MHC class I molecules-tapasin in the PLC and TAPBPR beyond.

ABSTRACT: Peptide loading of MHC-I molecules plays a critical role in the T cell response to infections and tumors as well as to interactions with inhibitory receptors on natural killer (NK) cells. To facilitate and optimize peptide acquisition, vertebrates have evolved specialized chaperones to stabilize MHC-I molecules during their biosynthesis and to catalyze peptide exchange favoring high affinity or optimal peptides to permit transport to the cell surface where stable peptide/MHC-I (pMHC-I) complexes are displayed and are available for interaction with T cell receptors and any of a host of inhibitory and activating receptors. Although components of the endoplasmic reticulum (ER) resident peptide loading complex (PLC) were identified some 30 years ago, the detailed biophysical parameters that go

SUBMITTER: Margulies DH 

PROVIDER: S-EPMC10308438 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature