Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates

Luca Tamagnone, Stefania Artigiani, Hang Chen, Zhigang He, Guo Li Ming, Hong Jun Song, Alain Chedotal, Margaret L. Winberg, Corey S. Goodman, Mu Ming Poo, Marc Tessier-Lavigne, Paolo M. Comoglio

Research output: Contribution to journalArticlepeer-review

Abstract

In Drosophila, plexin A is a functional receptor for semaphorin-1a. Here we show that the human plexin gene family comprises at least nine members in four subfamilies. Plexin-B1 is a receptor for the transmembrane semaphorin Sema4D (CD100), and plexin-C1 is a receptor for the GPI-anchored semaphorin Sema7A (Sema-K1). Secreted (class 3) semaphorins do not bind directly to plexins, but rather plexins associate with neuropilins, coreceptors for these semaphorins. Plexins are widely expressed: in neurons, the expression of a truncated plexin-A1 protein blocks axon repulsion by Sema3A. The cytoplasmic domain of plexins associates with a tyrosine kinase activity. Plexins may also act as ligands mediating repulsion in epithelial cells in vitro. We conclude that plexins are receptors for multiple (and perhaps all) classes of semaphorins, either alone or in combination with neuropilins, and trigger a novel signal transduction pathway controlling cell repulsion.

Original languageEnglish (US)
Pages (from-to)71-80
Number of pages10
JournalCell
Volume99
Issue number1
DOIs
StatePublished - Oct 1 1999
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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