Abstract:
:The MHC class I antigen presentation system enables T cell immunosurveillance of cancers and viruses. A substantial fraction of the immunopeptidome derives from rapidly degraded nascent polypeptides (DRiPs). By knocking down each of the 80 ribosomal proteins, we identified proteins that modulate peptide generation without altering source protein expression. We show that 60S ribosomal proteins L6 (RPL6) and RPL28, which are adjacent on the ribosome, play opposite roles in generating an influenza A virus-encoded peptide. Depleting RPL6 decreases ubiquitin-dependent peptide presentation, whereas depleting RPL28 increases ubiquitin-dependent and -independent peptide presentation. 40S ribosomal protein S28 (RPS28) knockdown increases total peptide supply in uninfected cells by increasing DRiP synthesis from non-canonical translation of "untranslated" regions and non-AUG start codons and sensitizes tumor cells for T cell targeting. Our findings raise the possibility of modulating immunosurveillance by pharmaceutical targeting ribosomes.
journal_name
Mol Celljournal_title
Molecular cellauthors
Wei J,Kishton RJ,Angel M,Conn CS,Dalla-Venezia N,Marcel V,Vincent A,Catez F,Ferré S,Ayadi L,Marchand V,Dersh D,Gibbs JS,Ivanov IP,Fridlyand N,Couté Y,Diaz JJ,Qian SB,Staudt LM,Restifo NP,Yewdell JWdoi
10.1016/j.molcel.2018.12.020subject
Has Abstractpub_date
2019-03-21 00:00:00pages
1162-1173.e5issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(18)31096-7journal_volume
73pub_type
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