Actinfilin, a brain-specific actin-binding protein in postsynaptic density
Actinfilin, a brain-specific actin-binding protein in postsynaptic density
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DOI：
10.1074/jbc.m202076200
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发表时间：
2002-08-23
影响因子：
4.8
通讯作者：
Li, M
中科院分区：
文献类型：
--
作者：
Chen, Y;Derin, R;Li, M
以肌动蛋白为基础的细胞骨架的动态组装和拆卸与突触后密度在数量和形状上的变化密切相关，这被认为是形成长期记忆的重要因素。因此，肌动蛋白丝的调节可能在促进长期记忆的形成中发挥关键作用。在这里，我们报告了肌动蛋白的克隆，肌动蛋白是一种脑特异性Kelch蛋白，与F-肌动蛋白相互作用。肌动蛋白含有一个氨基末端的POZ/BTB结构域和羧基定位的六个串联Kelch重复序列，这些重复序列可能形成Kelch结构域的六个β-螺旋桨结构的叶片。免疫共沉淀分析表明氨基端POZ结构域介导肌动蛋白-肌动蛋白相互作用。单独的重组Kelch结构域足以介导与F-肌动蛋白的结合。大鼠脑切片的免疫组织化学研究表明，肌动蛋白广泛表达于大脑大部分区域的神经元中。用生化分离和免疫金标记法研究了放线菌素的亚细胞定位。结果显示肌动蛋白在突触后的密度分布。总之，这些结果表明，肌动蛋白可能是肌动蛋白为基础的神经元功能的关键球员。
The dynamic assembly and disassembly of actin-based cytoskeleton is closely linked to the changes in the postsynaptic density in both number and shape, which is thought to be important in forming long-term memory. Thus, regulation of actin filaments may play a critical role in contributing to the formation of long-term memory. Here, we report the cloning of actinfilin, a brain-specific Kelch protein, which interacts with F-actin. Actinfilin contains an amino-terminal POZ/BTB domain and carboxyl positioned six tandem Kelch repeats that presumably form six blades of beta-propeller structure of the Kelch domain. Co-immunoprecipitation analyses showed that the amino-terminal POZ domain mediated actinfilin-actinfilin interaction. The recombinant Kelch domain alone was sufficient to mediate binding to F-actin. Immunohistochemistry studies of rat brain sections suggested that actinfilin is broadly expressed in neurons of most regions of the brain. The subcellular localization of actinfilin was studied by biochemical fractionation and immunogold labeling. The results showed the postsynaptic density distribution of actinfilin. Together, these results indicate that actinfilin may be a key player in the actin-based neuronal function.