| First Author | Gingras J | Year | 2016 |
| Journal | J Cell Sci | Volume | 129 |
| Issue | 5 | Pages | 898-911 |
| PubMed ID | 26769899 | Mgi Jnum | J:246102 |
| Mgi Id | MGI:5924562 | Doi | 10.1242/jcs.181180 |
| Citation | Gingras J, et al. (2016) Alpha-Dystrobrevin-1 recruits Grb2 and alpha-catulin to organize neurotransmitter receptors at the neuromuscular junction. J Cell Sci 129(5):898-911 |
| abstractText | Neuromuscular junctions (NMJs), the synapses made by motor neurons on muscle fibers, form during embryonic development but undergo substantial remodeling postnatally. Several lines of evidence suggest that alpha-dystrobrevin, a component of the dystrophin-associated glycoprotein complex (DGC), is a crucial regulator of the remodeling process and that tyrosine phosphorylation of one isoform, alpha-dystrobrevin-1, is required for its function at synapses. We identified a functionally important phosphorylation site on alpha-dystrobrevin-1, generated phosphorylation-specific antibodies to it and used them to demonstrate dramatic increases in phosphorylation during the remodeling period, as well as in nerve-dependent regulation in adults. We then identified proteins that bind to this site in a phosphorylation-dependent manner and others that bind to alpha-dystrobrevin-1 in a phosphorylation-independent manner. They include multiple members of the DGC, as well as alpha-catulin, liprin-alpha1, Usp9x, PI3K, Arhgef5 and Grb2. Finally, we show that two interactors, alpha-catulin (phosphorylation independent) and Grb2 (phosphorylation dependent) are localized to NMJs in vivo, and that they are required for proper organization of neurotransmitter receptors on myotubes. |
