New perspectives on the regulation of intermembrane glycerophospholipid traffic
New perspectives on the regulation of intermembrane glycerophospholipid traffic
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DOI：
10.1194/jlr.r200020-jlr200
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发表时间：
2003-03-01
影响因子：
6.5
通讯作者：
Voelker, DR
中科院分区：
文献类型：
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作者：
Voelker, DR
在真核生物中，磷脂酰丝氨酸（PtdSer）可以作为磷脂酰乙醇胺（PtdEtn）和磷脂酰胆碱（PtdCho）的前体，这是主要的细胞磷脂。PtdSer的合成起源于内质网（ER）及其亚结构域，称为内质网相关膜（MAM）。在哺乳动物细胞和酵母中，PtdSer被转运到线粒体，并被PtdSer脱羧酶1（Psd1p）脱羧形成PtdEtn。第二种脱羧酶Psd2p也存在于酵母的高尔基体液泡中。由Psd1p和Psd2p产生的PtdEtn可以被转运到ER，在那里它被甲基化形成PtdCho。细胞器特异性代谢的氨基甘油磷脂是一个强大的工具，实验以下的脂质交通，现在能够识别新的蛋白质参与调节这一过程。遗传和生物化学实验表明，MAM和线粒体之间的PtdSer的运输是由蛋白质泛素化，影响事件在两个膜调节。PtdSer运输到Psd2p位点的类似分析现在表明，膜结合的磷脂酰肌醇转移蛋白和Psd2p的C2结构域都需要在受体膜上用于PtdSer的有效运输。总之，这些最近的研究结果表明，供体和受体膜上的新型多蛋白组装体参与细胞器间磷脂转运。
In eukaryotes, phosphatidylserine (PtdSer) can serve as a precursor of phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho), which are the major cellular phospholipids. PtdSer synthesis originates in the endoplasmic reticulum (ER) and its subdomain named the mitochondria-associated membrane (MAM). PtdSer is transported to the mitochondria in mammalian cells and yeast, and decarboxylated by PtdSer decarboxylase 1 (Psd1p) to form PtdEtn. A second decarboxylase, Psd2p, is also found in yeast in the Golgi-vacuole. PtdEtn produced by Psd1p and Psd2p can be transported to the ER, where it is methylated to form PtdCho. Organelle-specific metabolism of the aminoglycerophospholipids is a powerful tool for experimentally following lipid traffic that is now enabling identification of new proteins involved in the regulation of this process. Genetic and biochemical experiments demonstrate that transport of PtdSer between the MAM and mitochondria is regulated by protein ubiquitination, which affects events at both membranes. Similar analyses of PtdSer transport to the locus of Psd2p now indicate that a membrane-bound phosphatidylinositol transfer protein and the C2 domain of Psd2p are both required on the acceptor membrane for efficient transport of PtdSer.jlr Collectively, these recent findings indicate that novel multiprotein assemblies on both donor and acceptor membranes participate in interorganelle phospholipid transport.