Faculty of Biochemistry, Chemistry and Pharmacy: Research Data

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Browsing Faculty of Biochemistry, Chemistry and Pharmacy: Research Data by Subject "mono-glucosylated N-glycan"

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  • Research Data
    Mechanism of the glycan-driven MHC I quality control cycle mediated by a dedicated chaperone network
    2025-04-24
    Heinke, Tim Julius 
    Fahim, Amin 
    Trowitzsch, Simon
    Tampé, Robert
    Heinke, Tim Julius  (DataCollector)
    Fahim, Amin  (DataCollector)
    Trowitzsch, Simon (ContactPerson)
    Tampé, Robert (ContactPerson)
    Protein folding in the endoplasmic reticulum (ER) is crucial for about one third of the mammalian proteome. N-linked glycosylation and subsequent restructuring of glycans barcodes glycoproteins during their maturation. UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) and the chaperones calnexin and calreticulin together with glucosidase I play a vital role in this process. MHC I molecules, key for adaptive immunity, additionally rely on the specialized chaperones tapasin and TAPBPR (TAP-binding protein-related) for their maturation and loading of antigenic peptides. Here, we delineate the functional interplay between tapasin, TAPBPR, UGGT1, and calreticulin, during recycling of MHC I molecules via purified components. The transfer of peptide-receptive MHC I from TAPBPR back to tapasin relies on the recognition of the mono-glucosylated glycan by calreticulin. Our findings unveil a finetuned dynamic network of glycan-dependent and MHC I-specific chaperones that guarantee maturation of MHC I molecules and highlight the fundamental processes driving ER protein quality control.
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