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

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Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation. / Trentini, Débora Broch; Pecoraro, Matteo; Tiwary, Shivani; Cox, Jürgen; Mann, Matthias; Hipp, Mark S; Hartl, F Ulrich.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 117, No. 8, 25.02.2020, p. 4099-4108.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Trentini, DB, Pecoraro, M, Tiwary, S, Cox, J, Mann, M, Hipp, MS & Hartl, FU 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, vol. 117, no. 8, pp. 4099-4108. https://doi.org/10.1073/pnas.1914401117

APA

Trentini, D. B., Pecoraro, M., Tiwary, S., Cox, J., Mann, M., Hipp, M. S., & Hartl, F. U. (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. https://doi.org/10.1073/pnas.1914401117

Vancouver

Trentini DB, Pecoraro M, Tiwary S, Cox J, Mann M, Hipp MS et al. 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. 2020 Feb 25;117(8):4099-4108. https://doi.org/10.1073/pnas.1914401117

Author

Trentini, Débora Broch ; Pecoraro, Matteo ; Tiwary, Shivani ; Cox, Jürgen ; Mann, Matthias ; Hipp, Mark S ; Hartl, F Ulrich. / Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation. In: Proceedings of the National Academy of Sciences of the United States of America. 2020 ; Vol. 117, No. 8. pp. 4099-4108.

Bibtex

@article{6cc3ee76107346829f3472ef3f7f5ddc,
title = "Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation",
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.",
author = "Trentini, {D{\'e}bora Broch} and Matteo Pecoraro and Shivani Tiwary and J{\"u}rgen Cox and Matthias Mann and Hipp, {Mark S} and Hartl, {F Ulrich}",
note = "Copyright {\textcopyright} 2020 the Author(s). Published by PNAS.",
year = "2020",
month = feb,
day = "25",
doi = "10.1073/pnas.1914401117",
language = "English",
volume = "117",
pages = "4099--4108",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "8",

}

RIS

TY - JOUR

T1 - Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation

AU - Trentini, Débora Broch

AU - Pecoraro, Matteo

AU - Tiwary, Shivani

AU - Cox, Jürgen

AU - Mann, Matthias

AU - Hipp, Mark S

AU - Hartl, F Ulrich

N1 - Copyright © 2020 the Author(s). Published by PNAS.

PY - 2020/2/25

Y1 - 2020/2/25

N2 - 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.

AB - 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.

U2 - 10.1073/pnas.1914401117

DO - 10.1073/pnas.1914401117

M3 - Journal article

C2 - 32047030

VL - 117

SP - 4099

EP - 4108

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 8

ER -

ID: 239206641