UBC
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
STAM2
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
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]
Throughput
- Low Throughput
Additional Notes
- #LPPI
- likely protein-protein interaction
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| STAM2 UBC | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 1108417 | |
| UBC STAM2 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | High | - | BioGRID | 2297218 |
Curated By
- BioGRID