The Phox Homology (PX) Domain
The Phox Homology (PX) Domain
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DOI：
10.1007/5584_2018_185
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发表时间：
2019-01-01
期刊：
影响因子：
--
通讯作者：
Collins, Brett M.
中科院分区：
文献类型：
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作者：
Chandra, Mintu;Collins, Brett M.
PX结构域是一个磷酸肌醇结合结构域，在所有真核生物中保守，存在于49种人类蛋白质中。含有PX结构域的蛋白质，其中许多也被称为分选连接蛋白（SNX），在与分泌和内吞系统的膜相关的膜运输、细胞信号传导和脂质代谢中具有多种功能。在这篇综述中，我们讨论了典型的脂质相互作用与内体富集的脂质磷脂酰肌醇-3-磷酸（PtdIns 3 P），以及非典型的脂质，促进膜协会的结构基础。我们还描述了最近的进展，在定义不同的机制，PX结构域与其他蛋白质，包括retromer运输复合物和细菌病原体分泌的蛋白质相互作用。像其他膜相互作用的结构域，PX结构域蛋白质的附着到特定的膜往往是由额外的相互作用，有助于结合亲和力，我们讨论了几个已知的例子，这种巧合检测。
The phox-homology (PX) domain is a phosphoinositide-binding domain conserved in all eukaryotes and present in 49 human proteins. Proteins containing PX domains, many of which are also known as sorting nexins (SNXs), have a large variety of functions in membrane trafficking, cell signaling, and lipid metabolism in association with membranes of the secretory and endocytic system. In this review we discuss the structural basis for both canonical lipid interactions with the endosome-enriched lipid phosphatidylinositol-3-phosphate (PtdIns3P) as well as non-canonical lipids that promote membrane association. We also describe recent advances in defining the diverse mechanisms by which PX domains interact with other proteins including the retromer trafficking complex and proteins secreted by bacterial pathogens. Like other membrane interacting domains, the attachment of PX domain proteins to specific membranes is often facilitated by additional interactions that contribute to binding avidity, and we discuss this coincidence detection for several known examples.