Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex.
Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex.
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DOI：
10.1083/jcb.200201037
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发表时间：
2002-04-01
影响因子：
7.8
通讯作者：
Bankaitis, Vytas A
中科院分区：
文献类型：
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作者：
Li, Xinmin;Rivas, Marcos P;Fang, Min;Marchena, Jennifer;Mehrotra, Bharat;Chaudhary, Anu;Feng, Li;Prestwich, Glenn D;Bankaitis, Vytas A
氧甾醇结合蛋白（OSBP）包含真核生物中一个大的保守蛋白家族。尽管它们无处不在，但这些蛋白质的功能活性仍然未知。 Kes1p 是酵母 OSBP 家族的七个成员之一，对高尔基复合体分泌功能进行负调节，该功能依赖于主要酵母磷脂酰肌醇/磷脂酰胆碱 Sec14p 的作用。我们现在证明 Kes1p 是酵母高尔基复合体的外周膜蛋白，Kes1p 在体内发挥功能需要定位到高尔基复合体，并且 Kes1p 靶向高尔基复合体需要与通过 Pik1p 作用生成的磷酸肌醇池结合，而不是与 Stt4p、PtdIns 4 激酶结合。 Kes1p 定位到酵母高尔基体区域还需要 OSBP 家族所有成员中发现的保守基序的功能。最后，我们提供的证据表明 Kes1p 可能调节酵母中的腺苷二磷酸核糖基化因子 (ARF) 功能，并且 Kes1p 可能通过改变 ARF 的调节与 Sec14p 相互作用来控制高尔基区的分泌功能。
Oxysterol binding proteins (OSBPs) comprise a large conserved family of proteins in eukaryotes. Their ubiquity notwithstanding, the functional activities of these proteins remain unknown. Kes1p, one of seven members of the yeast OSBP family, negatively regulates Golgi complex secretory functions that are dependent on the action of the major yeast phosphatidylinositol/phosphatidylcholine Sec14p. We now demonstrate that Kes1p is a peripheral membrane protein of the yeast Golgi complex, that localization to the Golgi complex is required for Kes1p function in vivo, and that targeting of Kes1p to the Golgi complex requires binding to a phosphoinositide pool generated via the action of the Pik1p, but not the Stt4p, PtdIns 4-kinase. Localization of Kes1p to yeast Golgi region also requires function of a conserved motif found in all members of the OSBP family. Finally, we present evidence to suggest that Kes1p may regulate adenosine diphosphate-ribosylation factor (ARF) function in yeast, and that it may be through altered regulation of ARF that Kes1p interfaces with Sec14p in controlling Golgi region secretory function.