Spatial organization of cofilin in dendritic spines
Spatial organization of cofilin in dendritic spines
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DOI：
10.1016/j.neuroscience.2005.11.025
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发表时间：
2006-01-01
期刊：
影响因子：
3.3
通讯作者：
Weinberg, RJ
中科院分区：
文献类型：
--
作者：
Racz, B;Weinberg, RJ
突触可塑性与树突棘的形态变化有关。以肌动蛋白为基础的细胞骨架在调节脊柱结构中起着关键作用，而脊椎中肌动蛋白的重组对于维持长时程增强至关重要。为了验证这样的假设，即稳定的F-肌动蛋白池位于脊柱的“核心”，而动态的F-肌动蛋白池位于其“壳”的外围，我们在大鼠海马体的放射层进行了免疫电子显微镜检查，以阐明cofilin的亚细胞分布，cofilin是一种肌动蛋白解聚蛋白，介导肌动蛋白细胞骨架的重组。我们提供的直接证据表明，脊椎中的粘附素避开了核心，而是集中在外壳和突触后密度内。这些数据表明，粘连蛋白可能将突触可塑性与肌动蛋白重塑联系在一起，肌动蛋白重塑是脊柱形态变化的基础。(C)2005年IBRO。爱思唯尔有限公司出版。保留所有权利。
Synaptic plasticity is associated with morphological changes in dendritic spines. The actin-based cytoskeleton plays a key role in regulating spine structure, and actin reorganization in spines is critical for the maintenance of long term potentiation. To test the hypothesis that a stable pool of F-actin rests in the spine "core," while a dynamic pool lies peripherally in its "shell," we performed immunoelectron microscopy in the stratum radiatum of rat hippocampus to elucidate the subcellular distribution of cofilin, an actin-depolymerizing protein that mediates reorganization of the actin cytoskeleton. We provide direct evidence that cofilin in spines avoids the core, and instead concentrates in the shell and within the postsynaptic density. These data suggest that cofilin may link synaptic plasticity to the actin remodeling that underlies changes in spine morphology. (c) 2005 IBRO. Published by Elsevier Ltd. All rights reserved.