| First Author | Proszynski TJ | Year | 2013 |
| Journal | J Cell Sci | Volume | 126 |
| Issue | Pt 10 | Pages | 2225-35 |
| PubMed ID | 23525008 | Mgi Jnum | J:349401 |
| Mgi Id | MGI:6791955 | Doi | 10.1242/jcs.121327 |
| Citation | Proszynski TJ, et al. (2013) Amotl2 interacts with LL5beta, localizes to podosomes and regulates postsynaptic differentiation in muscle. J Cell Sci 126(Pt 10):2225-35 |
| abstractText | Neuromuscular junctions (NMJs) in mammalian skeletal muscle undergo a postnatal topological transformation from a simple oval plaque to a complex branched structure. We previously showed that podosomes, actin-rich adhesive organelles, promote the remodeling process, and demonstrated a key role for one podosome component, LL5beta. To further investigate molecular mechanisms of postsynaptic maturation, we purified LL5beta-associated proteins from myotubes and showed that three regulators of the actin cytoskeleton--Amotl2, Asef2 and Flii--interact with LL5beta. These and other LL5beta-interacting proteins are associated with conventional podosomes in macrophages and podosome-like invadopodia in fibroblasts, strengthening the close relationship between synaptic and non-synaptic podosomes. We then focused on Amotl2, showing that it is associated with synaptic podosomes in cultured myotubes and with NMJs in vivo. Depletion of Amotl2 in myotubes leads to increased size of synaptic podosomes and corresponding alterations in postsynaptic topology. Depletion of Amotl2 from fibroblasts disrupts invadopodia in these cells. These results demonstrate a role for Amotl2 in synaptic maturation and support the involvement of podosomes in this process. |
