Identification of a conserved motif required for Vps35p/Vps26p interaction and assembly of the retromer complex
Résumé
The retromer complex is a conserved cytoplasmic coat complex that mediates the endosome-to-Golgi retrieval of vacuole/lysosome hydrolase receptors in yeast and mammals. The recognition of cargo proteins by retromer is performed by the Vps35p/VPS35 component which together with Vps26p/VPS26 and Vps29p/VPS29 forms the cargo-selective subcomplex. In this report we have identified a highly conserved region of Vps35p/VPS35 that is essential for the interaction with Vps26p/VPS26 and for assembly of the retromer complex. Mutation of residues within the conserved region results in mutants of Vps35p/VPS35 which cannot bind to Vps26p/VPS26 and are not efficiently targeted to the endosomal membrane. These data implicate Vps26p/VPS26 in regulating Vps35p/VPS35 membrane association and therefore suggest a role for Vps26p/VPS26 in cargo recognition.
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