Nuclear Hsp104 safeguards the dormant translation machinery during quiescence

Verena Kohler, Andreas Kohler, Lisa Larsson Berglund, Xinxin Hao, Sarah Gersing, Axel Imhof, Thomas Nyström, Johanna L. Höög, Martin Ott, Claes Andréasson () and Sabrina Büttner ()
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Verena Kohler: Stockholm University
Andreas Kohler: University of Graz
Lisa Larsson Berglund: University of Gothenburg
Xinxin Hao: University of Gothenburg
Sarah Gersing: University of Copenhagen
Axel Imhof: Ludwig Maximilian University of Munich
Thomas Nyström: University of Gothenburg
Johanna L. Höög: University of Gothenburg
Martin Ott: Stockholm University
Claes Andréasson: Stockholm University
Sabrina Büttner: Stockholm University

Nature Communications, 2024, vol. 15, issue 1, 1-20

Abstract: Abstract The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished.

Date: 2024
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DOI: 10.1038/s41467-023-44538-8

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