Regulation of cortical structure by the ezrin-radixin-moesin protein family
Regulation of cortical structure by the ezrin-radixin-moesin protein family
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DOI：
10.1016/s0955-0674(99)80013-1
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发表时间：
1999-02-01
影响因子：
7.5
通讯作者：
Bretscher, A
中科院分区：
文献类型：
--
作者：
Bretscher, A
已经鉴定了参与基于ERM（ezrin-radixin-moesin）的膜蛋白与细胞表面结构中的皮质细胞骨架的附着的分子。在淋巴细胞中，与细胞外基质受体和细胞间粘附分子直接相互作用。在极化上皮细胞中，名为EBP 50的衔接分子在埃兹蛋白的氨基末端结构域和质膜蛋白的胞质区域之间提供桥梁，包括囊性纤维化跨膜传导调节因子（CFTR）和β（2）肾上腺素能受体。ERM蛋白受到构象调节--EBP 50和F肌动蛋白的结合位点在休眠分子中被掩盖，激活会导致这些位点暴露。然而，激活的机制仍有待充分阐明。ERM蛋白还在Rho和Rac信号传导途径中发挥作用：活化的ERM蛋白可以将Rho-GDI（GDP解离抑制剂）从Rho解离，从而活化Rho依赖性途径。
Molecules involved in ERM (ezrin-radixin-moesin) based attachment of membrane proteins to the cortical cytoskeleton in cell surface structures have been identified. In lymphocytes, a direct interaction is seen with extracellular matrix receptors and intercellular adhesion molecules. In polarized epithelial cells, an adaptor molecule named EBP50 provides a bridge between the amino-terminal domain of ezrin and the cytoplasmic regions of plasma membrane proteins, including the cystic fibrosis transmembrane conductance regulator (CFTR) and the beta(2) adrenergic receptor. ERM proteins are conformationally regulated - binding sites for EBP50 and F actin are masked in the dormant molecules and activation leads to exposure of these sites. The mechanism of activation, however, remains to be fully elucidated. ERM proteins also play a role in the Rho and Rac signaling pathways: activated ERM proteins can dissociate Rho-GDI (GDP dissociation inhibitor) from Rho and thereby activate Rho-dependent pathways.