Determining how the GARP complex physically engages vesicles, the crystal structure of the Vps53 C-terminal domain revealed a tandem alpha-helical bundle fold with a conserved surface patch essential for binding endosome-derived vesicles, establishing VPS53 as a direct vesicle-contact subunit within multi-subunit tethering complexes.
Evidence X-ray crystallography at 2.9 Å resolution combined with site-directed mutagenesis and functional membrane traffic assays in yeast
- Identity of the vesicle-side receptor(s) recognized by the conserved surface patch is unknown
- Full-length VPS53 structure within the assembled GARP complex has not been determined
- Relative contributions of VPS53 versus other GARP subunits to vesicle capture remain unresolved