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Dynamics of DNA damage-induced nuclear inclusions are regulated by SUMOylation of Btn2

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  • Arun Kumar

    (675 West 10th Avenue
    University of British Columbia)

  • Veena Mathew

    (675 West 10th Avenue)

  • Peter C. Stirling

    (675 West 10th Avenue
    University of British Columbia)

Abstract

Spatial compartmentalization is a key facet of protein quality control that serves to store disassembled or non-native proteins until triage to the refolding or degradation machinery can occur in a regulated manner. Yeast cells sequester nuclear proteins at intranuclear quality control bodies (INQ) in response to various stresses, although the regulation of this process remains poorly understood. Here we reveal the SUMO modification of the small heat shock protein Btn2 under DNA damage and place Btn2 SUMOylation in a pathway promoting protein clearance from INQ structures. Along with other chaperones, and degradation machinery, Btn2-SUMO promotes INQ clearance from cells recovering from genotoxic stress. These data link small heat shock protein post-translational modification to the regulation of protein sequestration in the yeast nucleus.

Suggested Citation

  • Arun Kumar & Veena Mathew & Peter C. Stirling, 2024. "Dynamics of DNA damage-induced nuclear inclusions are regulated by SUMOylation of Btn2," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47615-8
    DOI: 10.1038/s41467-024-47615-8
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    References listed on IDEAS

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    1. Ibtissam Talhaoui & Manuel Bernal & Janet R. Mullen & Hugo Dorison & Benoit Palancade & Steven J. Brill & Gerard Mazón, 2018. "Slx5-Slx8 ubiquitin ligase targets active pools of the Yen1 nuclease to limit crossover formation," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    2. Liewei L. Yan & Carrie L. Simms & Fionn McLoughlin & Richard D. Vierstra & Hani S. Zaher, 2019. "Oxidation and alkylation stresses activate ribosome-quality control," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
    3. Irene Gallina & Camilla Colding & Peter Henriksen & Petra Beli & Kyosuke Nakamura & Judith Offman & David P. Mathiasen & Sonia Silva & Eva Hoffmann & Anja Groth & Chunaram Choudhary & Michael Lisby, 2015. "Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control," Nature Communications, Nature, vol. 6(1), pages 1-16, May.
    4. Chi-ting Ho & Tomas Grousl & Oren Shatz & Areeb Jawed & Carmen Ruger-Herreros & Marije Semmelink & Regina Zahn & Karsten Richter & Bernd Bukau & Axel Mogk, 2019. "Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
    5. Daniel Kaganovich & Ron Kopito & Judith Frydman, 2008. "Misfolded proteins partition between two distinct quality control compartments," Nature, Nature, vol. 454(7208), pages 1088-1095, August.
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