Open AccessStructure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes
Author(s) -
Neil Vasan,
Alex H. Hutagalung,
Peter Novick,
Karin M Reinisch
Publication year - 2010
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1009419107
Subject(s) - endosome , golgi apparatus , protein subunit , exocyst , biology , tethering , c terminus , vesicle , microbiology and biotechnology , n terminus , transport protein , peptide sequence , biochemistry , amino acid , membrane , gene , endoplasmic reticulum , intracellular
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 Å. We show that the C terminus consists of two α-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.