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A Conserved N‐terminal Arginine‐Motif in GOLPH3 ‐Family Proteins Mediates Binding to Coatomer
Author(s) -
Tu Linna,
Chen Lu,
Banfield David K.
Publication year - 2012
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2012.01403.x
Subject(s) - golgi apparatus , biology , microbiology and biotechnology , plasma protein binding , golgi membrane , binding site , biochemistry , endoplasmic reticulum
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 Vps 74p 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 Vps 74p largely account for the membrane‐binding capacity of the protein and identify an Arf 1p– Vps 74p interaction as a potential contributing factor in Vps 74p Golgi membrane association .