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TMT-based quantitative proteomics to study CHN-1/HSP-1 complex substrate turnover in C. elegans

ABSTRACT: The wild type (WT) and HSP-1 EEYD (worms generating endogenously mutated HSP-1) C. elegans were cultured under normal conditions (20 degrees) or exposed to 30 degrees for 16 hours as L4 larvae (referred to as heat stress/HS). In WT worms undergoing HS, the activity of CHN-1 ubiquitin ligase is anticipated to be inhibited by its interaction with wild-type HSP-1. In contrast, HSP-1 EEYD is expected not to inhibit CHN-1 in mutant worms, consequently leading to the degradation of a specific pool of proteins. This dataset unveils the identities of these proteins.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Caenorhabditis Elegans

TISSUE(S): Whole Body

SUBMITTER: Remigiusz Serwa

LAB HEAD: Wojciech Pokrzywa

PROVIDER: PXD048200 | Pride | 2024-11-08

REPOSITORIES: Pride

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			Action	DRS
	WP3_fr1_comparison_for_PCF.raw	Raw
	WP3_fr2_comparison_for_PCF.raw	Raw
	WP3_fr3_comparison_for_PCF.raw	Raw
	WP3_fr4_comparison_for_PCF.raw	Raw
	WP3_fr5_comparison_for_PCF.raw	Raw

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