Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors

被引:703
作者
Takahashi, T
Fournier, A
Nakamura, F
Wang, LH
Murakami, Y
Kalb, RG
Fujisawa, H
Strittmatter, SM [1 ]
机构
[1] Yale Univ, Sch Med, Dept Neurol, New Haven, CT 06510 USA
[2] Yale Univ, Sch Med, Neurobiol Sect, New Haven, CT 06510 USA
[3] Yale Univ, Sch Med, Dept Mol Cellular & Dev Biol, New Haven, CT 06510 USA
[4] Yale Univ, Sch Med, Dept Pharmacol, New Haven, CT 06510 USA
[5] Nagoya Univ, Grad Sch Sci, Grp Dev Neurobiol, Div Biol Sci, Nagoya, Aichi 4648602, Japan
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0092-8674(00)80062-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Class 1 and 3 semaphorins repulse axons but bind to different cell surface proteins. We find that the two known semaphorin-binding proteins, plexin 1 (Plex 1) and neuropilin-1 (NP-1), form a stable complex. Plex 1 alone does not bind semaphorin-3A (Sema3A), but the NP-1/Plex 1 complex has a higher affinity for Sema3A than does NP-1 alone. While Sema3A binding to NP-1 does not alter nonneuronal cell morphology, Sema3A interaction with NP-1/Plex 1 complexes induces adherent cells to round up. Expression of a dominant-negative Plex 1 in sensory neurons blocks Sema3A-induced growth cone collapse. Sema3A treatment leads to the redistribution of growth cone NP-1 and plexin into clusters. Thus, physiologic Sema3A receptors consist of NP-1/plexin complexes.
引用
收藏
页码:59 / 69
页数:11
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