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Structure of an MHC I–tapasin–ERp57 editing complex defines chaperone promiscuity

Author

Listed:
  • Ines Katharina Müller

    (Goethe University Frankfurt)

  • Christian Winter

    (Goethe University Frankfurt)

  • Christoph Thomas

    (Goethe University Frankfurt)

  • Robbert M. Spaapen

    (Sanquin Research
    University of Amsterdam)

  • Simon Trowitzsch

    (Goethe University Frankfurt)

  • Robert Tampé

    (Goethe University Frankfurt)

Abstract

Adaptive immunity depends on cell surface presentation of antigenic peptides by major histocompatibility complex class I (MHC I) molecules and on stringent ER quality control in the secretory pathway. The chaperone tapasin in conjunction with the oxidoreductase ERp57 is crucial for MHC I assembly and for shaping the epitope repertoire for high immunogenicity. However, how the tapasin–ERp57 complex engages MHC I clients has not yet been determined at atomic detail. Here, we present the 2.7-Å crystal structure of a tapasin–ERp57 heterodimer in complex with peptide-receptive MHC I. Our study unveils molecular details of client recognition by the multichaperone complex and highlights elements indispensable for peptide proofreading. The structure of this transient ER quality control complex provides the mechanistic basis for the selector function of tapasin and showcases how the numerous MHC I allomorphs are chaperoned during peptide loading and editing.

Suggested Citation

  • Ines Katharina Müller & Christian Winter & Christoph Thomas & Robbert M. Spaapen & Simon Trowitzsch & Robert Tampé, 2022. "Structure of an MHC I–tapasin–ERp57 editing complex defines chaperone promiscuity," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32841-9
    DOI: 10.1038/s41467-022-32841-9
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    1. Samoil Sekulovski & Pascal Devant & Silvia Panizza & Tasos Gogakos & Anda Pitiriciu & Katharina Heitmeier & Ewan Phillip Ramsay & Marie Barth & Carla Schmidt & Thomas Tuschl & Frank Baas & Stefan Weit, 2021. "Assembly defects of human tRNA splicing endonuclease contribute to impaired pre-tRNA processing in pontocerebellar hypoplasia," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    2. Huan Lan & Esam T. Abualrous & Jana Sticht & Laura Maria Arroyo Fernandez & Tamina Werk & Christoph Weise & Martin Ballaschk & Peter Schmieder & Bernhard Loll & Christian Freund, 2021. "Exchange catalysis by tapasin exploits conserved and allele-specific features of MHC-I molecules," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    3. Andreas Blees & Dovile Januliene & Tommy Hofmann & Nicole Koller & Carla Schmidt & Simon Trowitzsch & Arne Moeller & Robert Tampé, 2017. "Structure of the human MHC-I peptide-loading complex," Nature, Nature, vol. 551(7681), pages 525-528, November.
    4. Andrew C. McShan & Christine A. Devlin & Giora I. Morozov & Sarah A. Overall & Danai Moschidi & Neha Akella & Erik Procko & Nikolaos G. Sgourakis, 2021. "TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap," Nature Communications, Nature, vol. 12(1), pages 1-18, December.
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