Slit proteins bind robe receptors and have an evolutionarily conserved role in repulsive axon guidance

Slit proteins bind robe receptors and have an evolutionarily conserved role in repulsive axon guidance
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DOI:
10.1016/s0092-8674(00)80590-5
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发表时间:
1999-03-19
期刊:
影响因子:
64.5
通讯作者:
Kidd, T
Kidd, T
中科院分区:
生物学1区
文献类型:
--
作者:
Brose, K;Bland, KS;Kidd, T

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在发育中的神经系统中,轴突的延伸部分是由排斥信号引导的。在果蝇的遗传分析,在这篇论文的同伴报告,确定了裂缝蛋白作为一个候选配体的排斥指导受体回旋(机器人)。在这里,我们描述了三种哺乳动物Slit同源物的表征,并表明果蝇Slit蛋白和至少一种哺乳动物Slit蛋白,Slit 2,是蛋白水解加工的,并显示出特异性,高亲和力结合到长袍蛋白。此外,重组Slit2可以排斥细胞培养中的胚胎脊髓运动轴突。这些结果支持了这样的假设,即Slit蛋白作为长袍受体的排斥配体在轴突引导中具有进化上保守的作用。
Extending axons in the developing nervous system are guided in part by repulsive cues. Genetic analysis in Drosophila, reported in a companion to this paper, identifies the Slit protein as a candidate ligand for the repulsive guidance receptor Roundabout (Robo). Here we describe the characterization of three mammalian Slit homologs and show that the Drosophila Slit protein and at least one of the mammalian Slit proteins, Slit2, are proteolytically processed and show specific, high-affinity binding to Robe proteins. Furthermore, recombinant Slit2 can repel embryonic spinal motor axons in cell culture. These results support the hypothesis that Slit proteins have an evolutionarily conserved role in axon guidance as repulsive ligands for Robe receptors.