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  Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation

Broch Trentini, D., Pecoraro, M., Tiwary, S., Cox, J., Mann, M., Hipp, M. S., et al. (2020). Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 117(8), 4099-4108. doi:10.1073/pnas.1914401117.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-FB86-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-FB87-8
Genre: Journal Article

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 Creators:
Broch Trentini, Debora1, Author              
Pecoraro, Matteo2, Author              
Tiwary, Shivani3, Author              
Cox, Jürgen3, Author              
Mann, Matthias2, Author              
Hipp, Mark S.1, Author              
Hartl, F. Ulrich1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
3Cox, Jürgen / Computational Systems Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_2063284              

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Free keywords: COMBINED TRANSMEMBRANE TOPOLOGY; MESSENGER-RNA SURVEILLANCE; SIGNAL PEPTIDE PREDICTION; E3 UBIQUITIN LIGASE; ZIKA VIRUS; ENDONUCLEOLYTIC CLEAVAGE; STALLED RIBOSOME; MATURE PROTEINS; CELL-PROTEINS; ER MEMBRANEribosome-associated quality control; Listerin; MHC-I; immunopeptidome;
 Abstract: Mammalian cells present a fingerprint of their proteome to the adaptive immune system through the display of endogenous peptides on MHC-I complexes. MHC-I-bound peptides originate from protein degradation by the proteasome, suggesting that stably folded, long-lived proteins could evade monitoring. Here, we investigate the role in antigen presentation of the ribosome-associated quality control (RQC) pathway for the degradation of nascent polypeptides that are encoded by defective messenger RNAs and undergo stalling at the ribosome during translation. We find that degradation of model proteins by RQC results in efficient MHC-I presentation, independent of their intrinsic folding properties. Quantitative profiling of MHC-I peptides in wild-type and RQC-deficient cells by mass spectrometry showed that RQC substantially contributes to the composition of the immunopeptidome. Our results also identify endogenous substrates of the RQC pathway in human cells and provide insight into common principles causing ribosome stalling under physiological conditions.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000516771500034
DOI: 10.1073/pnas.1914401117
 Degree: -

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Title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Source Genre: Journal
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Publ. Info: 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA : NATL ACAD SCIENCES
Pages: - Volume / Issue: 117 (8) Sequence Number: - Start / End Page: 4099 - 4108 Identifier: ISSN: 0027-8424