Interaction of the C-terminal domain of δ glutamate receptor with spectrin in the dendritic spines of cultured Purkinje cells
Interaction of the C-terminal domain of δ glutamate receptor with spectrin in the dendritic spines of cultured Purkinje cells
复制标题
DOI：
10.1016/s0168-0102(99)00061-9
复制
发表时间：
1999-09-01
影响因子：
2.9
通讯作者：
Matsuda, S
中科院分区：
文献类型：
--
作者：
Hirai, H;Matsuda, S
神经递质受体通过突触下蛋白与细胞骨架的相互作用是中枢神经系统中受体靶向突触的重要机制。我们发现，δ谷氨酸受体（δ受体），主要表达在小脑浦肯野细胞的树突棘，直接与血影蛋白，肌动蛋白结合蛋白家族的成员。此外，血影蛋白和δ受体的C-末端结构域之间的相互作用在体外被1 μ M的Ca ~（2+）抑制50%，与没有Ca ~（2+）的情况相比。这些结果表明，小脑浦肯野细胞的树突棘突触后膜上的δ受体通过血影蛋白锚定到肌动蛋白细胞骨架，并且树突棘中的Ca 2+升高导致δ受体从血影蛋白解离。这种受体锚定在突触后位点的机制可以调节突触发生和/或突触可塑性。(C)1999爱思唯尔科学爱尔兰有限公司保留所有权利。
The interaction of neurotransmitter receptors with the underlying cytoskeleton via subsynaptic proteins is an important mechanism for the targeting of the receptors to synapses in the central nervous system. We show that delta glutamate receptors (delta receptors), expressed predominantly in the dendritic spines of cerebellar Purkinje cells, directly interact with spectrin, a member of the actin-binding family of proteins. Moreover, the interaction between spectrin and C-terminal domain of the delta receptor is 50% inhibited by 1 mu M of Ca2+ in vitro, compared with that in the absence of Ca2+. These results suggest that delta receptors on the postsynaptic membrane of the dendritic spines of cerebellar Purkinje cells are anchored to the actin cytoskeleton via spectrin, and that Ca2+ elevation in the dendritic spines causes delta receptor declustering by dissociation of the receptors from spectrin. This mechanism for receptor anchoring at postsynaptic sites may regulate synaptogenesis and/or synaptic plasticity. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved.