✦ LIBER ✦

Endosomal proteolysis and MHC class II function

✍ Scribed by Harold A Chapman

Publisher: Elsevier Science
Year: 1998
Tongue: English
Weight: 962 KB
Volume: 10
Category: Article
ISSN: 0952-7915
DOI: 10.1016/s0952-7915(98)80038-1

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✦ Synopsis

Newly synthesized MHC class II (x and 13 chains associate with a protein chaperone, the invariant chain, which promotes the proper assembly of MHC class II complexes and their trafficking through cells and prevents their untimely loading with peptides. Efficient loading of MHC class II heterodimers with antigenic peptides requires concurrent proteolytic processing of both the invariant chain and endocytosed proteins. Recent studies have elucidated the critical roles of specific cysteine proteases, especially cathepsins S and L, in degrading the invariant chain and regulating the convergence of processed antigen and MHC class II dimers competent for peptide loading.

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