IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-47615-8.html
   My bibliography  Save this article

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

Author

Listed:
  • 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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-47615-8
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-024-47615-8?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    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. 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.
    3. 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.
    4. 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.
    5. 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.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Arthur Fischbach & Angela Johns & Kara L. Schneider & Xinxin Hao & Peter Tessarz & Thomas Nyström, 2023. "Artificial Hsp104-mediated systems for re-localizing protein aggregates," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Yoshitaka Matsuo & Takayuki Uchihashi & Toshifumi Inada, 2023. "Decoding of the ubiquitin code for clearance of colliding ribosomes by the RQT complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Anne-Sophie Coquel & Jean-Pascal Jacob & Mael Primet & Alice Demarez & Mariella Dimiccoli & Thomas Julou & Lionel Moisan & Ariel B Lindner & Hugues Berry, 2013. "Localization of Protein Aggregation in Escherichia coli Is Governed by Diffusion and Nucleoid Macromolecular Crowding Effect," PLOS Computational Biology, Public Library of Science, vol. 9(4), pages 1-14, April.
    4. Melania Minoia & Jany Quintana-Cordero & Katharina Jetzinger & Ilgin Eser Kotan & Kathryn Jane Turnbull & Michela Ciccarelli & Anna E. Masser & Dorina Liebers & Eloïse Gouarin & Marius Czech & Vasili , 2024. "Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    5. Joana Silva & Ferhat Alkan & Sofia Ramalho & Goda Snieckute & Stefan Prekovic & Ana Krotenberg Garcia & Santiago Hernández-Pérez & Rob Kammen & Danielle Barnum & Liesbeth Hoekman & Maarten Altelaar & , 2022. "Ribosome impairment regulates intestinal stem cell identity via ZAKɑ activation," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. Sammy Villa & Pankaj Dwivedi & Aaron Stahl & Trent Hinkle & Christopher M. Rose & Donald S. Kirkpatrick & Seth M. Tomchik & Vishva M. Dixit & Fred W. Wolf, 2024. "OTUD6 deubiquitination of RPS7/eS7 on the free 40 S ribosome regulates global protein translation and stress," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47615-8. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.