Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

Publication

Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy.

Zavodszky E, Seaman MN, Moreau K, Jimenez-Sanchez M, Breusegem SY, Harbour ME, Rubinsztein DC

Endosomal protein sorting controls the localization of many physiologically important proteins and is linked to several neurodegenerative diseases. VPS35 is a component of the retromer complex, which mediates endosome-to-Golgi retrieval of membrane proteins such as the cation-independent mannose 6-phosphate receptor. Furthermore, retromer is also required for the endosomal recruitment of the actin nucleation promoting WASH complex. The VPS35 D620N mutation ... [more]

Nat Commun May. 13, 2014; 5();3828 [Pubmed: 24819384]

Throughput

Low Throughput

Additional Notes

Curated By

BioGRID

Interaction Summary

VPS35

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein binding [IPI]protein transporter activity [IBA]

Gene Ontology Cellular Component

ATG9A