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• W2086620006 abstract "The Saccharomyces cerevisiae phosphatidylcholine/phosphatidylinositol transfer protein Sec14p is required for Golgi apparatus-derived vesicular transport through coordinate regulation of phospholipid metabolism. Sec14p is normally essential. The essential requirement for SEC14 can be bypassed by inactivation of ( i ) the CDP–choline pathway for phosphatidylcholine synthesis or ( ii ) KES1 , which encodes an oxysterol binding protein. A unique screen was used to determine genome-wide genetic interactions for the essential gene SEC14 and to assess whether the two modes of “ sec14 bypass” were similar or distinct. The results indicate that inactivation of the CDP–choline pathway allows cells with inactivated SEC14 to live through a mechanism distinct from that of inactivation of KES1 . We go on to demonstrate an important biological function of Kes1p. Kes1p regulates Golgi apparatus-derived vesicular transport by inhibiting the function of Pik1p-generated Golgi apparatus phosphatidylinositol-4-phosphate (PI-4P). Kes1p affects both the availability and level of Golgi apparatus PI-4P. A set of potential PI-4P-responsive proteins that include the Rab GTPase Ypt31p and its GTP exchange factor are described." @default.
• W2086620006 created "2016-06-24" @default.
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• W2086620006 date "2007-09-25" @default.
• W2086620006 modified "2023-10-16" @default.
• W2086620006 title "The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function" @default.
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• W2086620006 doi "https://doi.org/10.1073/pnas.0705571104" @default.
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