The notion that alternative peptide substrates can be processed and presented to the MHC class I pathway has opened for new aspects on how the immune system detects infected or damaged cells. Recent works show that antigenic peptides are derived from intron sequences in pre-mRNAs target for the nonsense-mediated degradation pathway. Introns are spliced out co-transcriptionally suggesting that such pioneer translation products (PTPs) are synthesized on the nascent RNAs in the nuclear compartment to ensure that the first peptides to emerge from an mRNA are destined for the class I pathway. This illustrates an independent translation event during mRNA maturation that give rise to specific peptide products with a specific function in the immune system. The characterization of the translation apparatus responsible for PTP synthesis will pave the way for understanding how PTP production is regulated in different tissues under different conditions and will help designing new vaccine strategies.

Equipe Labellisée la Ligue Contre le Cancer Inserm UMR1162 Université Paris 7 Institut de Génétique Moléculaire 27 rue Juliette Dodu 75010 Paris France

Equipe Labellisée la Ligue Contre le Cancer Inserm UMR1162 Université Paris 7 Institut de Génétique Moléculaire 27 rue Juliette Dodu 75010 Paris France; RECAMO Masaryk Memorial Cancer Institute Zluty kopec 7 656 53 Brno Czech Republic

Institut Gustave Roussy Université Paris Sud Unité 1015 département d'immunologie 114 rue Edouard Vaillant 94805 Villejuif France

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An integrated DNA and RNA variant detector identifies a highly conserved three base exon in the MAP4K5 kinase locus