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

Fumio Nakamura, Masaki Tanaka, Takuya Takahashi, Robert G. Kalb, Stephen M. Strittmatter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

228 Scopus citations

Abstract

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, μ) 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.

Original languageEnglish (US)
Pages (from-to)1093-1100
Number of pages8
JournalNeuron
Volume21
Issue number5
DOIs
StatePublished - Nov 1998

ASJC Scopus subject areas

  • Neuroscience(all)

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