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.
© 2012 John Wiley & Sons A/S.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ADP-Ribosylation Factor 1 / metabolism
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Amino Acid Motifs
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Amino Acid Sequence
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Arginine / metabolism*
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Binding Sites
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Coatomer Protein / metabolism*
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Golgi Apparatus / metabolism
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Intracellular Membranes / metabolism
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Mannosyltransferases / metabolism
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Molecular Sequence Data
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Mutation
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Phosphatidylinositol Phosphates / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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Carrier Proteins
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Coatomer Protein
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Phosphatidylinositol Phosphates
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Saccharomyces cerevisiae Proteins
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Vps74 protein, S cerevisiae
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phosphatidylinositol 4-phosphate
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Arginine
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KRE2 protein, S cerevisiae
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Mannosyltransferases
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ADP-Ribosylation Factor 1