title: Transport and quality control of MHC class I molecules in the early secretory pathway.
abstract: Folding and peptide binding of major histocompatibility complex (MHC) class I molecules have been thoroughly researched, but the mechanistic connection between these biochemical events and the progress of class I through the early secretory pathway is much less well understood. This review focuses on the question how the partially assembled forms of class I (which lack high-affinity peptide and/or the light chain beta-2 microglobulin) are retained inside the cell. Such investigations offer researchers exciting chances to understand the connections between class I structure, conformational dynamics, peptide binding kinetics and thermodynamics, intracellular transport, and antigen presentation.
authors.affiliation: Jacobs University Bremen, Germany. Electronic address: sebastian.springer@queens.oxon.org.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Springer
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D015395:Histocompatibility Antigens Class I / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D017510:Protein Folding; D055571:Secretory Pathway
chemical_list: D015395:Histocompatibility Antigens Class I