Secreted chick semaphorins bind recombinant neuropilin with similar affinities but bind different subsets of neurons in situ
Secreted chick semaphorins bind recombinant neuropilin with similar affinities but bind different subsets of neurons in situ
复制标题
DOI：
10.1016/s0896-6273(00)80370-0
复制
发表时间：
1997-09-01
期刊：
影响因子：
16.2
通讯作者：
Raper, JA
中科院分区：
文献类型：
--
作者：
Feiner, L;Koppel, AM;Raper, JA
作为脑信号蛋白家族的一员，Collapsin-1激活特定生长锥上的受体，从而抑制它们的运动性。Neuropilin是一种以前克隆的跨膜蛋白，最近被鉴定为一个候选受体。我们已经完成了鸡的apopsin-3和-5的克隆，并显示apopsin-1，-2，-3，和-5绑定重叠，但不同的轴突束。我们推断，在原位，有不同的受体，具有不同的亲和力，为aprosin-1，-2，-3，和-5。相比之下，这四种蛋白酶都以相似的亲和力结合重组神经纤毛蛋白。与神经纤毛蛋白的强结合是由三分之一羧基介导的，而脑信号蛋白结构域赋予其独特的原位结合模式。我们建议，神经纤毛蛋白是一个共同的组成部分的脑信号蛋白受体复合物，和其他差异表达的受体成分与脑信号蛋白结构域相互作用，赋予结合特异性。
Collapsin-1, a member of the semaphorin family, activates receptors on specific growth cones, thereby inhibiting their motility. Neuropilin, a previously cloned transmembrane protein, has recently been identified as a candidate receptor for collapsin-1. We have completed the cloning of chick collapsin-3 and -5 and show that collapsin-1, -2, -3, and -5 bind to overlapping but distinct axon tracts. We infer that in situ, there are distinct receptors with different affinities for collapsin-1, -2, -3, and -5. In contrast, these four collapsins all bind recombinant neuropilin with similar affinities. Strong binding to neuropilin is mediated by the carboxy third of the collapsins, while the semaphorin domain confers their unique binding patterns in situ. We propose that neuropilin is a common component of a semaphorin receptor complex, and that additional differentially expressed receptor components interact with the semaphorin domains to confer binding specificity.