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Proximity labelling of pro-interleukin-1α reveals evolutionary conserved nuclear interactions

Author

Listed:
  • Rose Wellens

    (Manchester Academic Health Science Centre
    University of Manchester
    University of Manchester)

  • Victor S. Tapia

    (Manchester Academic Health Science Centre
    University of Manchester
    University of Manchester)

  • Paula I. Seoane

    (Manchester Academic Health Science Centre
    University of Manchester
    University of Manchester)

  • Hayley Bennett

    (University of Manchester)

  • Antony Adamson

    (University of Manchester)

  • Graham Coutts

    (Manchester Academic Health Science Centre
    University of Manchester
    University of Manchester)

  • Jack Rivers-Auty

    (University of Tasmania)

  • Martin Lowe

    (Manchester Academic Health Science Centre)

  • Jack P. Green

    (Manchester Academic Health Science Centre
    University of Manchester
    University of Manchester)

  • Gloria Lopez-Castejon

    (University of Manchester
    Manchester Academic Health Science Centre)

  • David Brough

    (Manchester Academic Health Science Centre
    University of Manchester
    University of Manchester)

  • Christopher Hoyle

    (Manchester Academic Health Science Centre
    University of Manchester
    University of Manchester)

Abstract

Interleukin-1α is a suggested dual-function cytokine that diverged from interleukin-1β in mammals potentially by acquiring additional biological roles that relate to highly conserved regions in the pro-domain of interleukin-1α, including a nuclear localisation sequence and histone acetyltransferase-binding domains. Why evolution modified pro-interleukin-1α’s subcellular location and protein interactome, and how this shaped interleukin-1α’s intracellular role, is unknown. Here we show that TurboID proximity labelling with pro-interleukin-1α suggests a nuclear role for pro-interleukin-1α that involves interaction with histone acetyltransferases, including EP300. We also identify and validate inactivating mutations in the pro-interleukin-1α nuclear localisation sequence of multiple mammalian species, including toothed whales, castorimorpha and marsupials. However, histone acetyltransferase-binding domains are conserved in those species that have lost pro-interleukin-1α nuclear localisation. Together, these data suggest that histone acetyltransferase binding and nuclear localisation occurred together, and that while some species lost the nuclear localisation sequence in their pro-interleukin-1α, histone acetyltransferase binding ability was maintained. The nuclear localisation sequence was lost from several distinct species at different evolutionary times, suggesting convergent evolution, and that the loss of the nuclear localisation sequence confers some important biological outcome.

Suggested Citation

  • Rose Wellens & Victor S. Tapia & Paula I. Seoane & Hayley Bennett & Antony Adamson & Graham Coutts & Jack Rivers-Auty & Martin Lowe & Jack P. Green & Gloria Lopez-Castejon & David Brough & Christopher, 2024. "Proximity labelling of pro-interleukin-1α reveals evolutionary conserved nuclear interactions," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-50901-0
    DOI: 10.1038/s41467-024-50901-0
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    References listed on IDEAS

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    1. Yang Zhou & Linda Shearwin-Whyatt & Jing Li & Zhenzhen Song & Takashi Hayakawa & David Stevens & Jane C. Fenelon & Emma Peel & Yuanyuan Cheng & Filip Pajpach & Natasha Bradley & Hikoyu Suzuki & Masato, 2021. "Platypus and echidna genomes reveal mammalian biology and evolution," Nature, Nature, vol. 592(7856), pages 756-762, April.
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