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Mitochondrial dysfunction rapidly modulates the abundance and thermal stability of cellular proteins

ABSTRACT: Cellular functionality relies on a well-balanced, but highly dynamic proteome. Dysfunctionof mitochondrial protein import leads to the cytosolic accumulation of mitochondrial precursor proteins which compromise cellular proteostasis and trigger the mitoprotein-induced stress response. To dissect the effects of mitochondrial dysfunction on the cellular proteome as a whole, we developed pre-post thermal proteome profiling (ppTPP). This multiplexed time-resolved proteome-wide thermal stability profiling approach with isobaric peptide tags in combination with a pulse SILAC labeling elucidated dynamic proteostasis changes in several dimensions: In addition to adaptations in protein abundance, we observed rapid modulations of the thermal stability of individual cellular proteins. Strikingly, different functional groups of proteins showed characteristic response patterns and reacted with group-specific kinetics, allowing the identification of the functional modules that are relevant for mitoprotein-induced stress. Thus, our new ppTPP approach uncovered a complex response network that orchestrates proteome homeostasis in eukaryotic cells by time-controlled adaptations of protein abundance and protein stability.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Frank Stein

LAB HEAD: Johannes M. Herrmann

PROVIDER: PXD037741 | Pride | 2023-02-21

REPOSITORIES: Pride

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			Action	DRS
	190402_light_only_merged_results_20190402_1343_peptides.txt	Txt
	190402_light_only_merged_results_20190402_1343_proteins.txt	Txt
	190402_light_only_merged_results_20190402_1343_summary.txt	Txt
	190402_light_only_merged_results_20190403_0334_peptides.txt	Txt
	190402_light_only_merged_results_20190403_0334_proteins.txt	Txt

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