Abstract
The yeast phosphatidylinositol transfer protein (Sec14p) is required for biogenesis of Golgi-derived transport vesicles and cell viability, and this essential Sec14p requirement is abrogated by inactivation of the CDP-choline pathway for phosphatidylcholine biosynthesis. These findings indicate that Sec14p functions to alleviate a CDP-choline pathway-mediated toxicity to yeast Golgi secretory function. We now report that this toxicity is manifested through the action of yeast Kes1p, a polypeptide that shares homology with the ligand-binding domain of human oxysterol binding protein (OSBP). Identification of Kes1p as a negative effector for Golgi function provides the first direct insight into the biological role of any member of the OSBP family, and describes a novel pathway for the regulation of Golgi-derived transport vesicle biogenesis.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alleles
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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Carrier Proteins / metabolism
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Cytidine Diphosphate Choline / metabolism
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DNA Primers
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism*
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Golgi Apparatus / physiology*
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Golgi Apparatus / ultrastructure
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Humans
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Membrane Proteins*
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Phosphatidylinositols / metabolism
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Phospholipid Transfer Proteins
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Polymerase Chain Reaction
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Receptors, Steroid / chemistry*
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / physiology*
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Saccharomyces cerevisiae / ultrastructure*
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
Substances
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Carrier Proteins
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DNA Primers
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Fungal Proteins
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KES1 protein, S cerevisiae
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Membrane Proteins
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Phosphatidylinositols
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Phospholipid Transfer Proteins
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Receptors, Steroid
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Recombinant Proteins
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SEC24 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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oxysterol binding protein
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Cytidine Diphosphate Choline