Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Mfn2 ubiquitination by PINK1/parkin gates the p97-dependent release of ER from mitochondria to drive mitophagy.

McLelland GL, Goiran T, Yi W, Dorval G, Chen CX, Lauinger ND, Krahn AI, Valimehr S, Rakovic A, Rouiller I, Durcan TM, Trempe JF, Fon EA

Despite their importance as signaling hubs, the function of mitochondria-ER contact sites in mitochondrial quality control pathways remains unexplored. Here we describe a mechanism by which Mfn2, a mitochondria-ER tether, gates the autophagic turnover of mitochondria by PINK1 and parkin. Mitochondria-ER appositions are destroyed during mitophagy, and reducing mitochondria-ER contacts increases the rate of mitochondrial degradation. Mechanistically, parkin/PINK1 catalyze a ... [more]

Elife Apr. 20, 2018; 7(); [Pubmed: 29676259]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • likely protein-protein interaction

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
UBC SHARPIN
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

High-BioGRID
2297336

Curated By

  • BioGRID