| First Author | Ayalon G | Year | 2008 |
| Journal | Cell | Volume | 135 |
| Issue | 7 | Pages | 1189-200 |
| PubMed ID | 19109891 | Mgi Jnum | J:150222 |
| Mgi Id | MGI:3849932 | Doi | 10.1016/j.cell.2008.10.018 |
| Citation | Ayalon G, et al. (2008) An ankyrin-based mechanism for functional organization of dystrophin and dystroglycan. Cell 135(7):1189-200 |
| abstractText | beta-dystroglycan (DG) and the dystrophin-glycoprotein complex (DGC) are localized at costameres and neuromuscular junctions in the sarcolemma of skeletal muscle. We present evidence for an ankyrin-based mechanism for sarcolemmal localization of dystrophin and beta-DG. Dystrophin binds ankyrin-B and ankyrin-G, while beta-DG binds ankyrin-G. Dystrophin and beta-DG require ankyrin-G for retention at costameres but not delivery to the sarcolemma. Dystrophin and beta-DG remain intracellular in ankyrin-B-depleted muscle, where beta-DG accumulates in a juxta-TGN compartment. The neuromuscular junction requires ankyrin-B for localization of dystrophin/utrophin and beta-DG and for maintenance of its postnatal morphology. A Becker muscular dystrophy mutation reduces ankyrin binding and impairs sarcolemmal localization of dystrophin-Dp71. Ankyrin-B also binds to dynactin-4, a dynactin subunit. Dynactin-4 and a subset of microtubules disappear from sarcolemmal sites in ankyrin-B-depleted muscle. Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4. |
