Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.
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.
Mesh Terms:
Animals, COS Cells, Ganglia, Spinal, Gene Expression, Growth Cones, Humans, Kidney, Multigene Family, Nerve Tissue Proteins, Neurons, Neuropilin-1, Protein Binding, Protein Structure, Tertiary, Receptors, Cell Surface, Signal Transduction, Solubility, Transfection
Animals, COS Cells, Ganglia, Spinal, Gene Expression, Growth Cones, Humans, Kidney, Multigene Family, Nerve Tissue Proteins, Neurons, Neuropilin-1, Protein Binding, Protein Structure, Tertiary, Receptors, Cell Surface, Signal Transduction, Solubility, Transfection
Cell
Date: Oct. 01, 1999
PubMed ID: 10520994
View in: Pubmed Google Scholar
Download Curated Data For This Publication
10952
Switch View:
- Interactions 5