A conserved N-terminal arginine-motif in GOLPH3-family proteins mediates binding to coatomer.

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.
Mesh Terms:
ADP-Ribosylation Factor 1, Amino Acid Motifs, Amino Acid Sequence, Arginine, Binding Sites, Carrier Proteins, Coatomer Protein, Golgi Apparatus, Intracellular Membranes, Mannosyltransferases, Molecular Sequence Data, Mutation, Phosphatidylinositol Phosphates, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
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Date: Nov. 01, 2012
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