Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin.
Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin.
复制标题
神经元支架蛋白亲旋蛋白丝状肌动蛋白结合域的结构功能分析。
DOI：
10.1111/j.1742-4658.2007.06171.x
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
Peti,Wolfgang
中科院分区：
文献类型：
--
作者：
Schüler,Herwig;Peti,Wolfgang
嗜棘蛋白是一种神经元支架蛋白，对突触传递至关重要，并将蛋白磷酸酶-1靶向树突棘中不同的亚细胞位置。它对调节树突棘的形成和运动至关重要，并通过调节β-amatergic受体和结合丝状肌动蛋白发挥作用。为了研究其在调节肌动蛋白细胞骨架结构中的作用，我们开始了亲棘素的肌动蛋白结合结构域的结构研究。我们证明，亲棘蛋白肌动蛋白结合域本质上是非结构化的，并且随着C末端长度的增加，该域显示出增强的二级结构内容。进一步表征证实了先前已知的交联活性，并发现了一种新的丝状肌动蛋白尖端封端活性。这两种功能似乎完全包含在亲棘素的残基1-154内。
Spinophilin, a neuronal scaffolding protein, is essential for synaptic transmission, and functions to target protein phosphatase‐1 to distinct subcellular locations in dendritic spines. It is vital for the regulation of dendritic spine formation and motility, and functions by regulating glutamatergic receptors and binding to filamentous actin. To investigate its role in regulating actin cytoskeletal structure, we initiated structural studies of the actin binding domain of spinophilin. We demonstrate that the spinophilin actin binding domain is intrinsically unstructured, and that, with increasing C‐terminal length, the domain shows augmented secondary structure content. Further characterization confirmed the previously known crosslinking activity and uncovered a novel filamentous actin pointed‐end capping activity. Both of these functions seem to be fully contained within residues 1–154 of spinophilin.