Abstract
AChR is concentrated at the postjunctional membrane at the neuromuscular junction. However, the underlying mechanism is unclear. We show that α-actinin, a protein known to cross-link F-actin, interacts with rapsyn, a scaffold protein essential for neuromuscular junction formation. α-Actinin, rapsyn, and surface AChR form a ternary complex. Moreover, the rapsyn-α-actinin interaction is increased by agrin, a factor known to stimulate AChR clustering. Downregulation of α-actinin expression inhibits agrin-mediated AChR clustering. Furthermore, the rapsyn-α-actinin interaction can be disrupted by inhibiting Abl and by cholinergic stimulation. Together these results indicate a role for α-actinin in AChR clustering.
Original language | English (US) |
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Pages (from-to) | 18 |
Number of pages | 1 |
Journal | Molecular brain |
Volume | 1 |
DOIs | |
State | Published - 2008 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Biology
- Cellular and Molecular Neuroscience