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1A GID E3 ligase assembly ubiquitinates an Rsp5 E3 adaptor and regulates plasma membrane transporters

ABSTRACT: Cells rapidly remodel their proteomes to align their cellular metabolism to environmentalconditions. Ubiquitin E3 ligases enablethis response, by facilitatingrapid andreversible changes to protein stability, localization, or interaction partners. In S. cerevisiae, the GID E3 ligase regulatesthe switch from gluconeogenic to glycolytic conditions throughinduction and incorporation of the substrate receptorsubunitGid4, whichpromotes the degradation of gluconeogenic enzymes. Here,we show an alternative substrate receptor, Gid10, which is induced in response to changes in temperature, osmolarity and nutrient availability,andregulates the ART-Rsp5 pathway. Art2 levels are elevated upon GID10deletion, a crystal structure shows the basis for Gid10-Art2 interactions, andGid10 directs a GID E3 ligase complex to ubiquitinate Art2. We also findthat the GID E3 ligase affects the flux of plasma membrane nutrient transportersduring heat stress. The data revealGID as a system of E3 ligases with metabolic regulatory functions outside of glycolysis and gluconeogenesis, controlled by distinct stress-specific substrate receptors.

INSTRUMENT(S): Q Exactive HF

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

SUBMITTER: Mario Oroshi

LAB HEAD: Matthias Mann

PROVIDER: PXD030902 | Pride | 2022-03-02

REPOSITORIES: Pride

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			Action	DRS
	20191018_QX4_OzKa_SA_GID10_proteome_1.raw	Raw
	20191018_QX4_OzKa_SA_GID10_proteome_10.raw	Raw
	20191018_QX4_OzKa_SA_GID10_proteome_11.raw	Raw
	20191018_QX4_OzKa_SA_GID10_proteome_12.raw	Raw
	20191018_QX4_OzKa_SA_GID10_proteome_13.raw	Raw

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