Palmitoylation plays a role in targeting Vac8p to specific membrane subdomains
Palmitoylation plays a role in targeting Vac8p to specific membrane subdomains
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DOI：
10.1111/j.1600-0854.2006.00472.x
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发表时间：
2006-10-01
期刊：
影响因子：
4.5
通讯作者：
Weisman, Lois S.
中科院分区：
文献类型：
--
作者：
Peng, Yutian;Tang, Fusheng;Weisman, Lois S.
Vac8p是一种多功能酵母蛋白，参与多种不同的液泡事件，包括液泡遗传、液泡同型融合、核-液泡连接形成和细胞质到液泡蛋白靶向途径。Vac8p通过肉豆蔻酰化和棕榈酰化与液泡膜结合。Vac8p有三个假定的棕榈酰化位点，分别是Cys 4、5和7。在这里，我们发现这些半胱氨酸中的每一个都可能作为棕榈酰化位点。单独在cys7上的棕榈酰化提供Vac8p的部分功能，而单独在cys4或cys5上的棕榈酰化足以实现Vac8p的功能。前者突变体Vac8p在液泡膜上的定位存在严重缺陷，后者突变体Vac8p在液泡膜上的定位存在部分缺陷。此外，我们的研究提供了棕榈酰化将Vac8p靶向到特定膜亚域的证据。
Vac8p is a multifunctional yeast protein involved in several distinct vacuolar events including vacuole inheritance, vacuole homotypic fusion, nucleus-vacuole junction formation and the cytoplasm to vacuole protein targeting pathway. Vac8p associates with the vacuole membrane via myristoylation and palmitoylation. Vac8p has three putative palmitoylation sites, at Cys 4, 5 and 7. Here, we show that each of these cysteines may serve as a palmitoylation site. Palmitoylation at Cys 7 alone provides partial function of Vac8p, whereas palmitoylation at either Cys 4 or Cys 5 alone is sufficient for Vac8p function. In the former mutant, there is a severe defect in the localization of Vac8p to the vacuole membrane, while in the latter mutants, there is a partial defect in the localization of Vac8p. In addition, our studies provide evidence that palmitoylation targets Vac8p to specific membrane subdomains.