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Coordination of translational control and protein homeostasis during severe heat stress

Background - Exposure of cells to severe heat stress causes not only misfolding and aggregation of proteins but also inhibition of translation and storage of mRNA in cytosolic heat stress granules (heat-SGs), limiting newly synthesized protein influx into overloaded proteome repair systems. How thes...

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Hauptverfasser: Khaimov, Valeria (VerfasserIn) , Hofmann, Sarah Ulrike (VerfasserIn) , Druffel-Augustin, Silke (VerfasserIn) , Mogk, Axel (VerfasserIn) , Tyedmers, Jens (VerfasserIn) , Stoecklin, Georg (VerfasserIn) , Bukau, Bernd (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: November 27, 2013
In: Current biology
Year: 2013, Jahrgang: 23, Heft: 24, Pages: 2452-2462
ISSN:1879-0445
DOI:10.1016/j.cub.2013.09.058
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.cub.2013.09.058
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0960982213012475
Volltext
Verfasserangaben:Valeria Cherkasov, Sarah Hofmann, Silke Druffel-Augustin, Axel Mogk, Jens Tyedmers, Georg Stoecklin, and Bernd Bukau
Beschreibung
Zusammenfassung:Background - Exposure of cells to severe heat stress causes not only misfolding and aggregation of proteins but also inhibition of translation and storage of mRNA in cytosolic heat stress granules (heat-SGs), limiting newly synthesized protein influx into overloaded proteome repair systems. How these two heat stress responses connect is unclear. - Results - Here, we show that both S. cerevisiae and D. melanogaster heat-SGs contain mRNA, translation machinery components (excluding ribosomes), and molecular chaperones and that heat-SGs coassemble with aggregates of misfolded, heat-labile proteins. Components in these mixed assemblies exhibit distinct molecular motilities reflecting differential trapping. We demonstrate that heat-SG disassembly and restoration of translation activity during heat stress recovery is intimately linked to disaggregation of damaged proteins present in the mixed assemblies and requires Hsp104 and Hsp70 activity. - Conclusions - Chaperone-driven protein disaggregation directly coordinates timing of translation reinitiation with protein folding capacity during cellular protein quality surveillance, enabling efficient protein homeostasis.
Beschreibung:Gesehen am 13.04.2021
Beschreibung:Online Resource
ISSN:1879-0445
DOI:10.1016/j.cub.2013.09.058

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