Plexin-Neuropilin-1 Complexes Form Functional Semaphorin-3A Receptors
Copyright policy )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.
- Department of Neurology Netherlands
- Yale University United States
- Nagoya University Japan
Neurons, Biochemistry, Genetics and Molecular Biology(all), Growth Cones, Gene Expression, Nerve Tissue Proteins, Receptors, Cell Surface, Kidney, Transfection, Neuropilin-1, Protein Structure, Tertiary, Solubility, Ganglia, Spinal, Multigene Family, COS Cells, Animals, Humans, Protein Binding, Signal Transduction
Neurons, Biochemistry, Genetics and Molecular Biology(all), Growth Cones, Gene Expression, Nerve Tissue Proteins, Receptors, Cell Surface, Kidney, Transfection, Neuropilin-1, Protein Structure, Tertiary, Solubility, Ganglia, Spinal, Multigene Family, COS Cells, Animals, Humans, Protein Binding, Signal Transduction
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