Journal
TRAFFIC
Volume 13, Issue 11, Pages 1496-1507Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1600-0854.2012.01403.x
Keywords
Arf1; COPI; glycosyltransferase; Golgi; Vps74p
Categories
Funding
- Research Grants Council of Hong Kong [660009, 660011]
- [HKUST6/CRF/08]
Ask authors/readers for more resources
Vps74p, a member of the GOLPH3 protein family, binds directly to coatomer and the cytoplasmic tails of a subset of Golgi-resident glycosyltransferases to mediate their Golgi retention. We identify a cluster of arginine residues at the N-terminal end of GOLPH3 proteins that are necessary and sufficient to mediate coatomer binding. While loss of coatomer binding renders Vps74p non-functional for glycosyltransferase retention, the Golgi membrane-binding capabilities of the mutant protein are not significantly reduced. We establish that the oligomerization status and phosphatidylinositol-4-phosphate-binding properties of Vps74p largely account for the membrane-binding capacity of the protein and identify an Arf1pVps74p interaction as a potential contributing factor in Vps74p Golgi membrane association.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available