Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse

被引：236

作者：

Nakamura, F ^{[1
]}

Tanaka, M ^{[1
]}

Takahashi, T ^{[1
]}

Kalb, RG ^{[1
]}

Strittmatter, SM ^{[1
]}

机构：

[1] Yale Univ, Sch Med, Dept Neurol, New Haven, CT 06510 USA

来源：

NEURON | 1998年 / 21卷 / 05期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0896-6273(00)80626-1

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Somatosensory axon outgrowth is repulsed when soluble semaphorin D (semD) binds to growth cone neuropilin-1 (Npn-1). Here, semD ligand binding studies of Npn-1 mutants demonstrate that the sema domain binds to the amino-terminal quarter, or complement-binding (CUB) domain, of Npn-1. By herpes simplex virus- (HSV-) mediated expression of Npn-1 mutants in chick retinal ganglion cells, we show that semD-induced growth cone collapse requires two segments of the ectodomain of Npn-1, the CUB domain and the juxtamembrane portion, or MAM (meprin, A5, mu) domain. In contrast, the transmembrane segment and cytoplasmic tail of Npn-1 are not required for biologic activity. These data imply that the CUB and MAM ectodomains of Npn-1 interact with another transmembrane growth cone protein that in turn transduces a semD signal into axon repulsion.

引用

页码：1093 / 1100

页数：8

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