Cellular and molecular interactions of phosphoinositides and peripheral proteins.
Cellular and molecular interactions of phosphoinositides and peripheral proteins.
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DOI：
10.1016/j.chemphyslip.2014.02.002
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发表时间：
2014-09
影响因子：
3.4
通讯作者：
Frick CT
中科院分区：
文献类型：
--
作者：
Stahelin RV;Scott JL;Frick CT
阴离子脂质充当将含有阳离子簇的蛋白质招募到生物膜的信号。被称为磷酸肌醇 (PIP) 的阴离子脂质家族丰度较低，但在将外周蛋白招募到膜界面方面发挥着关键作用。 PIP 是磷脂酰肌醇 (PI) 的单、双或三磷酸化衍生物，产生七种具有不同结构和阴离子电荷的物质。 PIP 的差异空间分布和时间外观是它们在向目标蛋白传递信息方面发挥作用的关键。 PIP 的选择性识别随着蛋白激酶 C 底物（称为 pleckstrin）拥有第一个 PIP 结合区域（称为 pleckstrin 同源 (PH) 结构域）的发现而发挥作用。自PH结构域发现以来，已鉴定出十多个PIP结合结构域，包括PH、ENTH、FYVE、PX和C2结构域。这些结构域中的每一个的代表性例子都已被彻底表征，以了解它们如何协调膜中的 PIP 头基、易位到细胞中的特定膜对接位点以及调节其全长蛋白活性的功能。此外，还出现了许多 PIP 介导的膜关联的新机制，例如重合检测——两个不同脂质头基的特异性。其他 PIP 结合域也可能对膜物理特性（例如电荷或膜曲率）具有选择性。这篇综述总结了目前对 PIP 的细胞分布及其与外周蛋白的分子相互作用的理解。
Anionic lipids act as signals for the recruitment of proteins containing cationic clusters to biological membranes. A family of anionic lipids known as the phosphoinositides (PIPs) are low in abundance, yet play a critical role in recruitment of peripheral proteins to the membrane interface. PIPs are mono-, bis-, or trisphosphorylated derivatives of phosphatidylinositol (PI) yielding seven species with different structure and anionic charge. The differential spatial distribution and temporal appearance of PIPs is key to their role in communicating information to target proteins. Selective recognition of PIPs came into play with the discovery that the substrate of protein kinase C termed pleckstrin possessed the first PIP binding region termed the pleckstrin homology (PH) domain. Since the discovery of the PH domain, more than ten PIP binding domains have been identified including PH, ENTH, FYVE, PX, and C2 domains. Representative examples of each of these domains have been thoroughly characterized to understand how they coordinate PIP headgroups in membranes, translocate to specific membrane docking sites in the cell, and function to regulate the activity of their full-length proteins. In addition, a number of novel mechanisms of PIP-mediated membrane association have emerged, such as coincidence detection – specificity for two distinct lipid headgroups. Other PIP-binding domains may also harbor selectivity for a membrane physical property such as charge or membrane curvature. This review summarizes the current understanding of the cellular distribution of PIPs and their molecular interaction with peripheral proteins.
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影响因子：
4.8
作者：
Adu-Gyamfi, Emmanuel;Soni, Smita P.;Stahelin, Robert V.
通讯作者：
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64.5
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11.8
作者：
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通讯作者：
Di Paolo, Gilbert
影响因子：
25
作者：
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通讯作者：
Di Paolo, Gilbert
影响因子：
3.5
作者：
Bolino, A;Brancolini, V;Devoto, M
通讯作者：
Devoto, M