| First Author | Glass DJ | Year | 1996 |
| Journal | Cell | Volume | 85 |
| Issue | 4 | Pages | 513-23 |
| PubMed ID | 8653787 | Mgi Jnum | J:33184 |
| Mgi Id | MGI:80664 | Doi | 10.1016/s0092-8674(00)81252-0 |
| Citation | Glass DJ, et al. (1996) Agrin acts via a MuSK receptor complex. Cell 85(4):513-23 |
| abstractText | Formation of th neuromuscular junction depends upon reciprocal inductive interactions between the developing nerve and muscle, resulting in the precise juxtaposition of a differentiated nerve terminal with a highly specialized patch on the muscle membrane, termed the motor endplate. Agrin is a nerve-derived factor that can induced molecular reorganizations at the motor endplate, but the mechanism of action of agrin remains poorly understood. MuSK is a receptor tyrosine kinase localized to the motor endplate, seemingly well positioned to receive a key nerve-derived signal. Mice lacking either agrin or MuSK have recently been generated and exhibit similarly profound defects in their neuromuscular junctions. Here we demonstrate that agrin acts via a receptor complex that includes MuSK as well as a myotube-specific accessory component. |
