Dynamics of the rapsyn scaffolding protein at the neuromuscular junction of live mice.
Dynamics of the rapsyn scaffolding protein at the neuromuscular junction of live mice.
复制标题
活体小鼠神经肌肉接头处 rapsyn 支架蛋白的动态。
DOI：
10.1523/jneurosci.4595-09.2010
复制
发表时间：
2010-01-13
影响因子：
5.3
通讯作者：
Akaaboune, Mohammed
中科院分区：
文献类型：
--
作者：
Bruneau, Emile G.;Akaaboune, Mohammed
突触传递的有效性依赖于突触后膜上神经递质受体及其相关支架蛋白的高密度维持。虽然受体的动力学已被广泛研究，但构成突触后密度的细胞内支架蛋白的动力学在体内基本上是未知的。在这里，我们专注于rapsyn的动态，所需的乙酰胆碱受体（AChR）的密度在突触后位点的集群和维护的蛋白质。使用延时成像，我们证明了rapsyn在功能性突触上与AChRs相比是非常动态的，翻转速度比AChRs快4-6倍。此外，我们发现rapsyn的快速更替对突触活动的变化不敏感，而AChR的更替受到深刻影响，这表明rapsyn和受体动态是由不同的机制控制的。这些数据表明，尽管突触结构总体稳定，但单个突触后成分是永久交换的，这可能在突触可塑性中起作用。
The efficacy of synaptic transmission depends on the maintenance of a high density of neurotransmitter receptors and their associated scaffold proteins in the postsynaptic membrane. While the dynamics of receptors has been extensively studied, the dynamics of the intracellular scaffold proteins that make up the postsynaptic density are largely unknown in vivo. Here, we focused on the dynamics of rapsyn, a protein required for the clustering and maintenance of acetylcholine receptor (AChR) density at postsynaptic sites. Using time-lapse imaging, we demonstrated that rapsyn is remarkably dynamic compared to AChRs at functional synapses, turning over 4-6 times more rapidly than AChRs. In addition we found that the rapid turnover of rapsyn is insensitive to alterations in synaptic activity, whereas AChR turnover is profoundly affected, illustrating that rapsyn and receptor dynamics are controlled by distinct mechanisms. These data indicate that individual postsynaptic components are in permanent exchange despite the overall stability of synaptic structure, which may play a role in synaptic plasticity.