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Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis

Author

Listed:
  • Chi-ting Ho

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

  • Tomas Grousl

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ)
    Institute of Microbiology of the Czech Academy of Sciences)

  • Oren Shatz

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

  • Areeb Jawed

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

  • Carmen Ruger-Herreros

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

  • Marije Semmelink

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

  • Regina Zahn

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

  • Karsten Richter

    (German Cancer Research Center (DKFZ))

  • Bernd Bukau

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

  • Axel Mogk

    (Center for Molecular Biology of Heidelberg University (ZMBH)
    German Cancer Research Center (DKFZ))

Abstract

Maintenance of cellular proteostasis is achieved by a multi-layered quality control network, which counteracts the accumulation of misfolded proteins by refolding and degradation pathways. The organized sequestration of misfolded proteins, actively promoted by cellular sequestrases, represents a third strategy of quality control. Here we determine the role of sequestration within the proteostasis network in Saccharomyces cerevisiae and the mechanism by which it occurs. The Hsp42 and Btn2 sequestrases are functionally intertwined with the refolding activity of the Hsp70 system. Sequestration of misfolded proteins by Hsp42 and Btn2 prevents proteostasis collapse and viability loss in cells with limited Hsp70 capacity, likely by shielding Hsp70 from misfolded protein overload. Btn2 has chaperone and sequestrase activity and shares features with small heat shock proteins. During stress recovery Btn2 recruits the Hsp70-Hsp104 disaggregase by directly interacting with the Hsp70 co-chaperone Sis1, thereby shunting sequestered proteins to the refolding pathway.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12868-1
    DOI: 10.1038/s41467-019-12868-1
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    Cited by:

    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. 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.
    3. 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.

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