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首页> 外文期刊>Biochemistry >Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: Regulation of the interactions by phosphatidylinositol-4,5-bisphosphate
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Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: Regulation of the interactions by phosphatidylinositol-4,5-bisphosphate

机译：红细胞β血影蛋白中的蛋白质4.1R和肌动蛋白结合位点的鉴定和功能表征：磷脂酰肌醇-4,5-双磷酸酯相互作用的调节

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摘要

The ternary complex of spectrin, F-actin, and protein 4.1R defines the erythrocyte membrane skeletal network, which governs the stability and elasticity of the membrane. It has been shown that both 4.1R and actin bind to the N-terminal region (residues 1-301) of the spectrin beta chain, which contains two calponin homology domains, designated CH1 and CH2. Here, we show that 4.1R also binds to the separate CH1 and CH2 domains. Unexpectedly, truncation of the CH2 domain by its 20 amino acids, corresponding to its N-terminal a helix, was found to greatly enhance its binding to 4.1R. The intact N terminus and the CH1 but not the CH2 domain bind to F-actin, but again, deletion of the first 20 amino acids of the latter exposes an actin-binding activity. As expected, the polypeptide 1-301 inhibits the binding of spectrin dimer to actin and formation of the spectrin-actin-4.1R ternary complex in vitro. Furthermore, the binding of 4.1R to 1-301 is greatly enhanced by PIP2, implying the existence of a regulatory switch in the cell.
机译：血影蛋白，F-肌动蛋白和蛋白质4.1R的三元复合物定义了红细胞膜骨架网络，该网络控制着膜的稳定性和弹性。已经显示4.1R和肌动蛋白都结合到血影蛋白β链的N-末端区域（残基1-301），其包含两个钙蛋白同源域，称为CH1和CH2。在这里，我们显示4.1R还绑定到单独的CH1和CH2域。出乎意料的是，发现CH2结构域被其20个氨基酸（对应于其N末端螺旋）截短可大大增强其与4.1R的结合。完整的N末端和CH1但不与CH2结构域结合到F-肌动蛋白，但是同样，后者的前20个氨基酸的缺失暴露了肌动蛋白的结合活性。如所预期的，多肽1-301在体外抑制血影蛋白二聚体与肌动蛋白的结合以及血影蛋白-肌动蛋白-4.1R三元复合物的形成。此外，PIP2大大增强了4.1R与1-301的结合，这表明细胞中存在调节开关。

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