Diversity of phosphoinositide binding proteins in Entamoeba histolytica
Diversity of phosphoinositide binding proteins in Entamoeba histolytica
复制标题
溶组织内阿米巴中磷酸肌醇结合蛋白的多样性
DOI：
10.1016/j.parint.2021.102367
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发表时间：
2021
影响因子：
1.9
通讯作者：
Nozaki Tomoyoshi
中科院分区：
文献类型：
--
作者：
Watanabe Natsuki;Nakada-Tsukui Kumiko;Nozaki Tomoyoshi
磷脂酰肌醇磷酸盐(PIP)定位于所有细胞室的膜上，在多种细胞事件中起着关键作用。位于特定细胞器或膜结构域的PIP通过选择性地与单个或一组PIP结合的蛋白结构域，以时空特异性的方式结合和招募各种蛋白质，从而实现其功能。在溶组织内阿米巴，人类肠道原虫寄生虫，PIPs和PIP结合蛋白已被证明参与其毒力相关的机制，如细胞运动，囊泡运输，特罗戈和吞噬。在电子搜索中搜索与PIP绑定有关的域和签名。组织溶解蛋白质组可以鉴定数十种潜在的PIP结合蛋白。然而，这样的分析往往是误导的，除非谨慎地选择用作查询的蛋白质结构域，并通过实验验证蛋白质的结合特异性。这是因为最初假定与其他系统中的PIP结合的所有结构域并不总是能够与PIP结合，而是参与其他生物角色。在这篇综述中，我们对含有PIP结合域的蛋白质进行了电子扫描。仅利用已被实验证明是忠实的PIP结合生物探针的有效的PIP结合域。我们的调查发现，含有FYVE(FAB1、YOTB1、Vac1、EEA1)和PH(Pleckstrin Homology)结构域的蛋白是扩展最多的家族。组织溶血剂。一些含有FYVE结构域的蛋白(EhFP4和10)和含有Phox同源(Px)结构域的蛋白(EhSNX1和2)已被深入研究。组织溶血剂。此外，大多数已鉴定的含有PH结构域的蛋白都被注释为蛋白激酶，并具有蛋白激活域。总体而言，可以通过使用具有良好特性的生物探针的结构域对基因组进行电子扫描来鉴定的PIP结合结构域包含的蛋白质是有限的。组织溶血剂。然而，它们的结构域结构通常是独特的，这表明在这种有机体中，含有PIP结合结构域的蛋白质具有独特的进化。
Phosphatidylinositol phosphates (PIPs, phosphoinositides) are localized to the membranes of all cellular compartments, and play pivotal roles in multiple cellular events. To fulfill their functions, PIPs that are located to specific organelles or membrane domains bind to and recruit various proteins in spatiotemporal specific manner via protein domains that selectively bind to either a single or an array of PIPs. InEntamoeba histolytica, the human intestinal protozoan parasite, PIPs and PIP-binding proteins have been shown to be involved in their virulence-associated mechanisms such as cell motility, vesicular traffic, trogo- and phagocytosis. In silico search of the domains and the signatures implicated in PIP binding in theE. histolyticaproteome allows identification of dozens of potential PIP-binding proteins. However, such analysis is often misleading unless the protein domain used as query is cautiously selected and the binding specificity of the proteins are experimentally validated. This is because all the domains initially presumed to bind PIPs in other systems are not always capable of PIP binding, but rather involved in other biological roles. In this review, we carried out in silico survey of proteins which have PIP-binding domains in theE. histolyticagenome by utilizing only validated PIP-binding domains that had been experimentally proven to be faithful PIP-binding bioprobes. Our survey has identified that FYVE (Fab1, YOTB1, Vac1, EEA1) and PH (pleckstrin homology) domain containing proteins are the most expanded families inE. histolytica. A few FYVE domain-containing proteins (EhFP4 and 10) and phox homology (PX) domain containing proteins (EhSNX1 and 2) were previously studied in depth inE. histolytica. Furthermore, most of the identified PH domain-containing proteins are annotated as protein kinases and possess protein kinase domains. Overall, PIP-binding domain-containing proteins that can be identified by in silico survey of the genome using the domains from well characterized bioprobes are limited inE. histolytica. However, their domain architectures are often unique, suggesting unique evolution of PIP-binding domain-containing proteins in this organism.