A change in the selective translocation of the Kinesin-1 motor domain marks the initial specification of the axon
A change in the selective translocation of the Kinesin-1 motor domain marks the initial specification of the axon
复制标题
DOI：
10.1016/j.neuron.2006.02.005
复制
发表时间：
2006-03-16
期刊：
影响因子：
16.2
通讯作者：
Banker, GA
中科院分区：
文献类型：
--
作者：
Jacobson, C;Schnapp, B;Banker, GA
我们使用运动域中结构性活性运动蛋白的积累来衡量运动蛋白在发育中的神经元中的移位。在整个发育过程中，截短的Kinesin-3在所有神经突起的顶端积累。相反，激动素-1只选择性地积聚在神经突起的一个子集中。在神经元极化之前，截短的Kinesin-1在单个轴突中短暂积累。与轴突规范一致的是，截短的Kinesin-1只在新生的轴突中积聚，不再出现在任何其他轴突中。Kinesin-1沿着通往新生轴突的生化轨道的移位可以确保Kinesin-1货物选择性地输送到轴突，从而有助于其分子规范。对YFP标记的截断Kinesin-1进行成像，可以提供迄今为止最精确的神经元极性首次出现的定义，并允许实时可视化轴突的分子分化。
We used the accumulation of constitutively active kinesin motor domains as a measure of where kinesins translocate in developing neurons. Throughout development, truncated Kinesin-3 accumulates at the tips of all neurites. In contrast, Kinesin-1 selectively accumulates in only a subset of neurites. Before neurons become polarized, truncated Kinesin-1 accumulates transiently in a single neurite. Coincident with axon specification, truncated Kinesin-1 accumulates only in the emerging axon and no longer appears in any other neurite. The translocation of Kinesin-1 along a biochemically distinct track leading to the nascent axon could ensure the selective delivery of Kinesin-1 cargoes to the axon and hence contribute to its molecular specification. Imaging YFP-tagged truncated Kinesin-1 provides the most precise definition to date of when neuronal polarity first emerges and allows visualization of the molecular differentiation of the axon in real time.