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Discreet and distinct clustering of five model membrane proteins revealed by single molecule localization microscopy.
Molecular Membrane Biology ( IF 2.857 ) Pub Date : 2015-06-26 , DOI: 10.3109/09687688.2014.990997
Astrid Magenau 1 , Dylan M Owen , Yui Yamamoto , Jason Tran , Joanna M Kwiatek , Robert G Parton , Katharina Gaus
Affiliation  

Compartmentalization is a functionally important property of the plasma membrane, yet the underlying principles that organize membrane proteins into distinct domains are not well understood. Using single molecule localization microscopy, we assessed the clustering of five model membrane proteins in the plasma membrane of HeLa cells. All five proteins formed discrete and distinct nano-scaled clusters. The extent of clustering of the five proteins, independent of their membrane anchors, increased significantly when the fluorescent protein mEOS2 was employed, suggesting that protein–protein interactions are a key driver for clustering. Further, actin depolymerization or reduction of membrane order had a greater, and in some instances opposing effects on the clustering of membrane proteins fused to mEOS2 compared to PS-CFP2-fusion proteins. The data propose that protein interactions can override the lateral organization imposed by membrane anchors to provide an exquisite regulation of the mosaic-like compartmentalization of the plasma membrane.



中文翻译:

单分子定位显微镜揭示的五个模型膜蛋白的离散和独特的群集。

隔室化是质膜的功能上重要的性质,但是将膜蛋白组织成不同结构域的基本原理还没有被很好地理解。使用单分子定位显微镜,我们评估了五个模型膜蛋白在HeLa细胞质膜中的聚集。所有五个蛋白质形成离散且不同的纳米级簇。当使用荧光蛋白mEOS2时,这5种蛋白的簇集程度与膜锚无关,而显着增加,这表明蛋白与蛋白的相互作用是簇集的关键驱动力。此外,与PS-CFP2融合蛋白相比,肌动蛋白解聚或膜顺序降低更大,并且在某些情况下,对融合于mEOS2的膜蛋白簇的作用相反。

更新日期:2015-06-26
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