Asparagine endopeptidase can initiate the removal of the MHC class II invariant chain chaperone

Benedicte Manoury, Daniela Mazzeo, Dongtao Ni Li, Jeremy Billson, Kylie Loak, Philippe Benaroch, Colin Watts

    Research output: Contribution to journalArticle

    83 Citations (Scopus)

    Abstract

    The invariant chain (Ii) chaperone for MHC class II molecules is crucial for their effective function. Equally important is its removal. Cathepsins S or L are known to be required for the final stages of Ii removal in different APCs, but the enzymes which initiate Ii processing have not been identified. Here we show that this step can be performed in B lymphocytes by asparagine endopeptidase (AEP), which targets different asparagine residues in the lumenal domain of human and mouse invariant chain. Inhibition of AEP activity slows invariant chain processing and hinders the expression of an antigenic peptide engineered to replace the groove binding region of Ii (CLIP). However, the initiation of Ii removal can also be performed by other proteases, reflecting the importance of this step.
    Original languageEnglish
    Pages (from-to)489-498
    Number of pages10
    JournalImmunity
    Volume18
    Issue number4
    DOIs
    Publication statusPublished - 2003

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