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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Focal Adhesion Proteins Connect Ige Receptors To The Cytoskeleton As Revealed By Micropatterned Ligand Arrays
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Focal Adhesion Proteins Connect Ige Receptors To The Cytoskeleton As Revealed By Micropatterned Ligand Arrays

机译：局部黏附蛋白将Ige受体连接到细胞骨架，如微模式配体阵列所揭示的那样

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摘要

Patterned surfaces that present specific ligands in spatially defined arrays are used to examine structural linkages between clustered IgE receptors (IgE-FcεRI) and the cytoskeleton in rat basophilic leukemia (RBL) mast cells. We showed with fluorescence microscopy that cytoskeletal F-actin concentrates in the same regions as cell surface IgE-FcεRI that bind to the micrometer-size patterned ligands. However, the proteins mediating these cytoskeletal connections and their functional relevance were not known. We now show that whereas the adaptor proteins ezrin and moesin do not detectably concentrate with the array of clustered IgE-FcεRI, focal adhesion proteins vinculin, paxillin, and talin, which are known to link F-actin with integrins, accumulate in these regions on the same time scale as F-actin. Moreover, colocalization of these focal adhesion proteins with clustered IgE-FcεRI is enhanced after addition of fibronectin-RGD peptides. Significantly, the most prominent rat basophilic leukemia cell integrin (α5) avoids the patterned regions occupied by the ligands and associates preferentially with exposed regions of the silicon substrate. Thus, spatial separation provided by the patterned surface reveals that particular focal adhesion proteins, which connect to the actin cytoskeleton, associate with ligand-cross-linked IgE-FcεRI, independently of integrins. We investigated the functional role of one of these proteins, paxillin, in IgE-FcεRI-mediated signaling by using small interfering RNA. From these results, we determine that paxillin reduces stimulated phos-phorylation of the FcεRI β subunit but enhances stimulated Ca~(2+) release from intracellular stores. The results suggest that paxillin associated with clustered IgE-FcεRI has a net positive effect on FcεRI signaling.
机译：在空间定义的阵列中呈现特定配体的图案化表面用于检查成簇的IgE受体（IgE-FcεRI）与大鼠嗜碱性白血病（RBL）肥大细胞中细胞骨架之间的结构联系。我们用荧光显微镜显示，细胞骨架F-肌动蛋白集中在与细胞表面IgE-FcεRI相同的区域，该区域结合到微米尺寸的图案化配体上。但是，介导这些细胞骨架连接及其功能相关性的蛋白质尚不清楚。我们现在显示，尽管衔接蛋白ezrin和moesin不能与成簇的IgE-FcεRI阵列可检测地浓缩，但是粘着斑蛋白vinculin，paxillin和talin（已知将F-actin与整联蛋白连接）聚集在这些区域上。与F-肌动蛋白的时间比例相同。此外，添加纤连蛋白-RGD肽后，这些粘着斑蛋白与成簇的IgE-FcεRI的共定位得到增强。重要的是，最突出的大鼠嗜碱性白血病细胞整联蛋白（α5）避免了被配体占据的图案化区域，并优先与硅基质的暴露区域缔合。因此，由图案化表面提供的空间分离揭示了与肌动蛋白细胞骨架相连的特定的粘着斑蛋白，独立于整联蛋白而与配体交联的IgE-FcεRI缔合。我们通过使用小分子干扰RNA，研究了其中一种蛋白paxillin在IgE-FcεRI介导的信号传导中的功能作用。从这些结果，我们确定帕西林减少了FcεRIβ亚基的刺激的磷酸化，但是增加了从细胞内存储释放的刺激的Ca〜（2+）。结果表明，与簇状的IgE-FcεRI相关的paxillin对FcεRI信号传导具有净阳性作用。

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