| First Author | Hu H | Year | 2011 |
| Journal | Neurosci Lett | Volume | 489 |
| Issue | 1 | Pages | 10-5 |
| PubMed ID | 21129441 | Mgi Jnum | J:168704 |
| Mgi Id | MGI:4936784 | Doi | 10.1016/j.neulet.2010.11.056 |
| Citation | Hu H, et al. (2011) Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression. Neurosci Lett 489(1):10-5 |
| abstractText | Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of alpha-dystroglycan (alpha-DG) exhibit defective photoreceptor synaptic function. Mouse knockouts of dystroglycan and its extracellular matrix binding partner pikachurin recapitulate this phenotype. In this study, pikachurin-alpha-dystroglycan interactions in several mouse models of CMD were examined by pikachurin overlay experiments. The results show that hypoglycosylation of alpha-dystroglycan resulted in markedly reduced pikachurin-alpha-dystroglycan interactions. Expression of pikachurin is abolished at the outer plexiform layer of two mouse models, protein O-mannose N-acetylglucosaminyl transferase 1 (POMGnT1) knockout and Large(myd) mice. Overexpressing LARGE restored this interaction in POMGnT1 knockout cells. These results indicate that pikachurin interactions with alpha-dystroglycan and its localization at the photoreceptor ribbon synapse require normal glycosylation of alpha-dystroglycan. |
