Identification of a conserved motif required for Vps35p/Vps26p interaction and assembly of the retromer complex

Suzanne Gokool , Daniel Tattersall , Jonathan V Reddy , Matthew N Seaman (1)

1 CIMR - Cambridge Institute for Medical Research

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.

Mots clés: Life Sciences

Suzanne Gokool, Daniel Tattersall, Jonathan V Reddy, Matthew N Seaman. Identification of a conserved motif required for Vps35p/Vps26p interaction and assembly of the retromer complex. Biochemical Journal, 2007, 408 (2), pp.287-295. ⟨10.1042/BJ20070555⟩. ⟨hal-00478792⟩