Fig. 3: Ssa1 T492 phosphorylation fine-tunes the epichaperome.
From: Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response
a Proteomic workflow. WT and T492A Ssa1 complexes were purified from heat-shocked yeast, and epichaperome changes were quantified using mass spectrometry. Created in BioRender. Truman, A. (2025) https://BioRender.com/24ppob4b Volcano plot of epichaperome changes between WT and T492A cells. The log2 change (WT/T492A) and p-value for each interactor are plotted from the values obtained from 3 biological replicates. Statistical significance was determined by ANOVA. c GO analysis of WT vs T492A epichaperome based on cellular processes. d GO analysis of WT vs T492A epichaperome based on cellular localization. e T492 phosphorylation preferentially alters interaction with proteins of low disorder. Number of disordered proteins that significantly changed interaction with Ssa1 (log2 WT/A value > 1 or < − 1) vs unchanged. f T492 phosphorylation alters the interaction between Ssa1 and major chaperone and co-chaperone proteins. The 15 chaperones and co-chaperones were grouped by homology and function and then colored based on the interaction change between WT and T492A samples.
