Amotl2 interacts with LL5β, localizes to podosomes and regulates postsynaptic differentiation in muscle.

ABSTRACT: 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, LL5β. To further investigate molecular mechanisms of postsynaptic maturation, we purified LL5β-associated proteins from myotubes and showed that three regulators of the actin cytoskeleton--Amotl2, Asef2 and Flii--interact with LL5β. These and other LL5β-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

SUBMITTER: Proszynski TJ 

PROVIDER: S-EPMC3672938 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature