Membrane phosphatidylserine regulates surface charge and protein localization
Membrane phosphatidylserine regulates surface charge and protein localization
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DOI：
10.1126/science.1152066
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发表时间：
2008-01-11
期刊：
影响因子：
56.9
通讯作者：
Grinstein, Sergio
中科院分区：
文献类型：
--
作者：
Yeung, Tony;Gilbert, Gary E.;Grinstein, Sergio
与带负电荷的膜的静电相互作用有助于具有多元簇或阳离子结构域的蛋白质的亚细胞靶向。虽然阴离子磷脂磷脂酰丝氨酸相对丰富，但其对单个细胞膜表面电荷的贡献尚不清楚，部分原因是缺乏分析其在完整细胞中分布的试剂。我们开发了一种生物传感器来研究磷脂酰丝氨酸的亚细胞分布，发现它结合质膜的胞质小叶，以及内体和溶酶体。与磷脂酰丝氨酸的存在相关的负电荷将具有中等正电荷的蛋白导向内吞途径。更强烈的阳离子蛋白，通常与质膜，重新定位到内吞隔室时，质膜表面电荷减少钙内流。
Electrostatic interactions with negatively charged membranes contribute to the subcellular targeting of proteins with polybasic clusters or cationic domains. Although the anionic phospholipid phosphatidylserine is comparatively abundant, its contribution to the surface charge of individual cellular membranes is unknown, partly because of the lack of reagents to analyze its distribution in intact cells. We developed a biosensor to study the subcellular distribution of phosphatidylserine and found that it binds the cytosolic leaflets of the plasma membrane, as well as endosomes and lysosomes. The negative charge associated with the presence of phosphatidylserine directed proteins with moderately positive charge to the endocytic pathway. More strongly cationic proteins, normally associated with the plasma membrane, relocalized to endocytic compartments when the plasma membrane surface charge decreased on calcium influx.