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- W1502316579 abstract "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 Arf1p–Vps74p interaction as a potential contributing factor in Vps74p Golgi membrane association." @default.
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- W1502316579 date "2012-09-04" @default.
- W1502316579 modified "2023-10-01" @default.
- W1502316579 title "A Conserved N-terminal Arginine-Motif in GOLPH3-Family Proteins Mediates Binding to Coatomer" @default.
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- W1502316579 doi "https://doi.org/10.1111/j.1600-0854.2012.01403.x" @default.
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