pH-susceptibility of HLA-DO tunes DO/DM ratios to regulate HLA-DM catalytic activity
نویسندگان
چکیده
منابع مشابه
Transmembrane domain-mediated colocalization of HLA-DM and HLA-DR is required for optimal HLA-DM catalytic activity.
HLA-DM catalyzes peptide loading and exchange reactions by MHC class II molecules. Soluble recombinant DM, lacking transmembrane and cytoplasmic domains, was observed to have 200- to 400-fold less activity compared with the full-length protein in assays measuring DM-catalyzed peptide dissociation from purified HLA-DR1 in detergent solutions. Additional studies with truncated soluble DR1 demonst...
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Recent studies have revealed that the conserved major histocompatibility complex class II molecule, HLA-DO, inhibits the class II antigen-processing pathway. HLA-DO, expressed in only a subset of antigen-presenting cells, binds HLA-DM and blocks HLA-DM-catalyzed peptide loading of class II molecules.
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In multivesicular bodies, HLA-DM (DM) assists the loading of antigenic peptides on classical MHC class II molecules such as HLA-DR. In cells expressing HLA-DO (DO), DM is redistributed from the internal vesicles to the limiting membrane of these organelles. This suggests that DO might reduce DM incorporation into exosomes, which are shed upon fusion of multivesicular bodies with the plasma memb...
متن کاملHLA-DO is a negative modulator of HLA-DM-mediated MHC class II peptide loading
BACKGROUND Class II molecules of the major histocompatibility complex become loaded with antigenic peptides after dissociation of invariant chainderived peptides (CLIP) from the peptide-binding groove. The human leukocyte antigen (HLA)-DM is a prerequisite for this process, which takes place in specialised intracellular compartments. HLA-DM catalyses the peptide-exchange process, simultaneously...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2015
ISSN: 2045-2322
DOI: 10.1038/srep17333