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首页> 外文期刊>Biochemistry >Insights into a single rod-like helix in activated radixin required for membrane-cytoskeletal cross-linking
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Insights into a single rod-like helix in activated radixin required for membrane-cytoskeletal cross-linking

机译：洞察细胞膜-骨架交联所需的激活的放射性单棒状螺旋

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The members of the ezrin-radixin-moesin (ERM) family of proteins function as membrane-cytoskeletal cross-linkers in actin-rich cell surface structures. ERM proteins are thereby thought to be essential for cortical cytoskeleton organization, cell motility, adhesion, and proliferation. These modular polypeptides consist of a central helix-rich region, termed the alpha-domain, that connects an N-terminal FERM domain required for membrane binding and a C-terminal region which contains a major actin-binding motif. Conformational regulation of ERM protein function occurs by association of the FERM and C-terminal domains, whereby the membrane- and actin-binding activities are mutually suppressed and the protein is thought to take an inactive "closed" form. Here we report in vitro and in vivo studies of radixin to address the role of the alpha-domain in conformational activation of ERM proteins. Remarkably, an isolated alpha-domain comprised of radixin(311-469) forms a monomeric, stable helical rod that spans 240 Angstrom in length from the N-terminus to the C-terminus, most likely stabilized by extensive salt bridge interactions. By fusing green fluorescent protein variants to the FERM and C-terminal domains, we probed in vitro conformational changes impacted by the presence of the alpha-domain using fluorescence resonance energy transfer (FRET). Furthermore, deletion of this unusually long alpha-helical structure (radixin residues 314-411) prevents ERM membrane targeting in vivo. [References: 28]
机译：ezrin-radixin-moesin（ERM）蛋白家族的成员在富含肌动蛋白的细胞表面结构中充当膜-细胞骨架交联剂。因此，ERM蛋白被认为是皮质细胞骨架组织，细胞运动，粘附和增殖所必需的。这些模块化多肽由称为α-结构域的中央螺旋丰富区域组成，该区域连接膜结合所需的N-末端FERM结构域和包含主要肌动蛋白结合基序的C-末端区域。 ERM蛋白功能的构象调节是通过FERM和C末端结构域的结合而发生的，因此膜和肌动蛋白的结合活性被相互抑制，并且该蛋白被认为是非活性的“封闭”形式。在这里，我们报告了对Radixin的体外和体内研究，以解决α结构域在ERM蛋白构象活化中的作用。值得注意的是，由radixin（311-469）组成的分离的α结构域形成了一个单体的，稳定的螺旋棒，从N端到C端的长度为240埃，很可能通过广泛的盐桥相互作用而稳定下来。通过将绿色荧光蛋白变体融合到FERM和C末端结构域，我们使用荧光共振能量转移（FRET）探测了受α结构域影响的体外构象变化。此外，这种异常长的α-螺旋结构（放射蛋白残基314-411）的缺失阻止了ERM膜在体内的靶向。 [参考：28]

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