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

Takuya Takahashi, Alyson Fournier, Fumio Nakamura, Li Hsien Wang, Yasunori Murakami, Robert G. Kalb, Hajime Fujisawa, Stephen M. Strittmatter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

680 Scopus citations

Abstract

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 I 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.

Original languageEnglish (US)
Pages (from-to)59-69
Number of pages11
JournalCell
Volume99
Issue number1
DOIs
StatePublished - Oct 1 1999

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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