Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes.
The Golgi-associated retrograde protein (GARP) complex is a membrane-tethering complex that functions in traffic from endosomes to the trans-Golgi network. Here we present the structure of a C-terminal fragment of the Vps53 subunit, important for binding endosome-derived vesicles, at a resolution of 2.9 A. We show that the C terminus consists of two alpha-helical bundles arranged in tandem, and we identify a highly conserved surface patch, which may play a role in vesicle recognition. Mutations of the surface result in defects in membrane traffic. The fold of the Vps53 C terminus is strongly reminiscent of proteins that belong to three other tethering complexes--Dsl1, conserved oligomeric Golgi, and the exocyst--thought to share a common evolutionary origin. Thus, the structure of the Vps53 C terminus suggests that GARP belongs to this family of complexes.
Vasan
Neil
N
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA.
Hutagalung
Alex
A
Novick
Peter
P
Reinisch
Karin M
KM
D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D011992:Endosomes / Q000378:metabolism; D046912:Multiprotein Complexes / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D021122:Protein Subunits; D021381:Protein Transport; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D021601:trans-Golgi Network / Q000378:metabolism*
D002352:Carrier Proteins; D046912:Multiprotein Complexes; D010446:Peptide Fragments; D021122:Protein Subunits; D029701:Saccharomyces cerevisiae Proteins; C492177:VPS53 protein, S cerevisiae