Neurexin mediates the assembly of presynaptic terminals
Neurexin mediates the assembly of presynaptic terminals
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DOI：
10.1038/nn1074
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发表时间：
2003-07-01
影响因子：
25
通讯作者：
Scheiffele, P
中科院分区：
文献类型：
--
作者：
Dean, C;Scholl, FG;Scheiffele, P
神经毒素是作为神经元细胞表面受体的蛋白质的大家族。然而，各种neurexins的功能和定位尚未明确。β-神经毒素是神经连接素-1的候选受体，神经连接素-1是一种突触后膜蛋白，可以在轴突接触处触发突触形成。在这里，我们报告，neurexins集中在突触和纯化的neuroligin是足够的集群neurexin和诱导突触前分化。神经连接素的寡聚化是其功能所必需的，我们发现β-neurexin聚集足以通过需要neurexin胞质结构域的相互作用触发突触囊泡的募集。我们提出了一个两步模型，其中突触后神经连接素多聚体最初集群轴突神经毒素。响应于这种聚集，neurexins使细胞质支架的组装成核，胞吐器被募集到该细胞质支架。
Neurexins are a large family of proteins that act as neuronal cell-surface receptors. The function and localization of the various neurexins, however, have not yet been clarified. Beta-neurexins are candidate receptors for neuroligin-1, a postsynaptic membrane protein that can trigger synapse formation at axon contacts. Here we report that neurexins are concentrated at synapses and that purified neuroligin is sufficient to cluster neurexin and to induce presynaptic differentiation. Oligomerization of neuroligin is required for its function, and we find that beta-neurexin clustering is sufficient to trigger the recruitment of synaptic vesicles through interactions that require the cytoplasmic domain of neurexin. We propose a two-step model in which postsynaptic neuroligin multimers initially cluster axonal neurexins. In response to this clustering, neurexins nucleate the assembly of a cytoplasmic scaffold to which the exocytotic apparatus is recruited.