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A metabolite sensor subunit of the Atg1/ULK complex regulates selective autophagy; whole cell proteome

ABSTRACT: Cells convert complex metabolic information into stress-adapted autophagy responses. Canonically, multilayered protein kinase networks converge on the conserved Atg1/ULK kinase complex (AKC) to induce non-selective and selective forms of autophagy in response to metabolic changes. Here, we show that, upon phosphate starvation, the metabolite sensor Pho81 interacts with the adaptor subunit Atg11 at the AKC via an Atg11/FIP200 interaction motif to modulate pexophagy by virtue of its conserved phospho-metabolite sensing SPX domain. Notably, core AKC components Atg13 and Atg17 are dispensable for phosphate starvation-induced autophagy revealing significant compositional and functional plasticity of the AKC. Our data indicate that, instead of functioning as a selective autophagy receptor, Pho81 compensates for partially inactive Atg13 by promoting Atg11-phosphorylation by Atg1 critical for pexophagy during phosphate starvation. Our work shows Atg11/FIP200 adaptor subunits not only bind selective autophagy receptors but also modulator subunits that convey metabolic information directly to the AKC for autophagy regulation.

INSTRUMENT(S): Orbitrap Fusion Lumos

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

SUBMITTER: Ilian Atanassov

LAB HEAD: Martin Graef

PROVIDER: PXD048176 | Pride | 2023-12-31

REPOSITORIES: Pride

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			Action	DRS
	MaxQuant_plus_database.7z	Other
	d_atg11_d_pho81_proteome_PD_output.7z	Other
	d_atg11_d_pho81_proteome_data_analysis.7z	Other
	d_atg11_d_pho81_proteome_raw_data.7z	Other
	d_atg1_d_atg11_proteome_MaxQuant_output.7z	Other

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