SNARE蛋白Ykt6在同型液泡融合的早期阶段介导蛋白质棕榈酰化。
The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion.
作者信息
Dietrich Lars E P, Gurezka Rolf, Veit Michael, Ungermann Christian
机构信息
Biochemie-Zentrum Heidelberg (BZH), University of Heidelberg, Heidelberg, Germany.
出版信息
EMBO J. 2004 Jan 14;23(1):45-53. doi: 10.1038/sj.emboj.7600015. Epub 2003 Dec 11.
Abstract
The NSF homolog Sec18 initiates fusion of yeast vacuoles by disassembling cis-SNARE complexes during priming. Sec18 is also required for palmitoylation of the fusion factor Vac8, although the acylation machinery has not been identified. Here we show that the SNARE Ykt6 mediates Vac8 palmitoylation and acts during a novel subreaction of vacuole fusion. This subreaction is controlled by a Sec17-independent function of Sec18. Our data indicate that Ykt6 presents Pal-CoA via its N-terminal longin domain to Vac8, while transfer to Vac8's SH4 domain occurs spontaneously and not enzymatically. The conservation of Ykt6 and its localization to several organelles suggest that its acyltransferase activity may also be required in other intracellular fusion events.
摘要
NSF 同源物 Sec18 在引发过程中通过拆解顺式 SNARE 复合体启动酵母液泡融合。融合因子 Vac8 的棕榈酰化也需要 Sec18，尽管酰化机制尚未明确。在这里，我们表明 SNARE 蛋白 Ykt6 介导 Vac8 的棕榈酰化，并在液泡融合的一个新的子反应中发挥作用。这个子反应由 Sec18 的一个不依赖 Sec17 的功能控制。我们的数据表明，Ykt6 通过其 N 端的长链结构域将棕榈酰辅酶 A 呈递给 Vac8，而向 Vac8 的 SH4 结构域的转移是自发的，并非酶促反应。Ykt6 的保守性及其在多个细胞器中的定位表明，其酰基转移酶活性可能在其他细胞内融合事件中也有需求。
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