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DM and DO shape the repertoire of peptide–MHC-class-II complexes

✍ Scribed by Lars Karlsson

Publisher
Elsevier Science
Year
2005
Tongue
English
Weight
117 KB
Volume
17
Category
Article
ISSN
0952-7915

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✦ Synopsis

The presentation of antigenic peptides by MHC class II molecules is essential for activation of CD4+ T cells. The formation of most peptide-MHC-class-II complexes is influenced by the actions of two specialized accessory proteins--DM and DO--located in the endosomal/lysosomal system where peptide loading occurs. DM removes class-II-associated invariant-chain peptide (CLIP) from newly synthesized class II molecules, but by now it is clearly established that this is only a special case of the general peptide-editing function of DM. Recent data have begun to explain the molecular basis for the editing activity. The other accessory protein, DO, modulates DM activity in vitro, but the physiological importance of DO is unclear. New evidence from several laboratories has provided clues that may soon change this.

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