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 language | English (US) |
|---|---|
| Pages (from-to) | 59-69 |
| Number of pages | 11 |
| Journal | Cell |
| Volume | 99 |
| Issue number | 1 |
| DOIs | |
| State | Published - Oct 1 1999 |
Funding
We thank M. Tessier-Lavigne for providing the AP-Sema3F expression vector. This work was supported by grants to S. M. S. from the National Institutes of Health and the American Paralysis Association. S. M. S. is a John Merck Scholar in the Biology of Developmental Disorders in Children and an Investigator of the Patrick and Catherine Weldon Donaghue Medical Research Foundation. A. F. is supported by a FCAR research fellowship. F. N. is supported by a research fellowship from the Spinal Cord Research Fund of the Paralyzed Veterans of America.
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology