MassIVE MSV000096492

Complete Public PXD058151

Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response

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Description

Yeast must respond rapidly to heat stress by activating multiple signaling pathways that preserve proteostasis. This includes induction of Hsf1 and Msn2/4-mediated transcription, cell integrity signaling, stress-triggered phase separation of proteins and inhibition of translation. How these pathways are so rapidly activated and co-ordinated remains unclear. We show that the mechanosensor Mid2 senses heat-induced membrane stretch and leads to rapid phosphorylation of the cytosolic Hsp70 Ssa1 at a well-conserved threonine (T492). Phosphorylation of T492 leads to epichaperome rearrangement which includes altered interaction with Hsf1, multiple ribosomal subunits, the Bck1 MEK, and Edc3. Taken together these results provide a comprehensive, unified theory of the global yeast shock response that is mediated by the Hsp70 chaperone code. [doi:10.25345/C51C1TT2N] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: heat shock response ; yeast ; Hsp70 ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		Luca Fornelli, University of Oklahoma, United States
Submitting User: Fornelli_Lab
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