The myotubularin-amphiphysin 2 complex in membrane tubulation and centronuclear myopathies.
Myotubularin (MTM1) and amphiphysin 2 (BIN1) are two proteins mutated in different forms of centronuclear myopathy, but the functional and pathological relationship between these two proteins was unknown. Here, we identified MTM1 as a novel binding partner of BIN1, both in vitro and endogenously in skeletal muscle. Moreover, MTM1 enhances ... BIN1-mediated membrane tubulation, depending on binding and phosphoinositide phosphatase activity. BIN1 patient mutations induce a conformational change in BIN1 and alter its binding and regulation by MTM1. In conclusion, we identified the first molecular and functional link between MTM1 and BIN1, supporting a common pathological mechanism in different forms of centronuclear myopathy.
Mesh Terms:
Animals, COS Cells, Cell Membrane, Cercopithecus aethiops, Mice, Muscle, Skeletal, Myopathies, Structural, Congenital, Nerve Tissue Proteins, Phosphoric Monoester Hydrolases, Protein Binding, Protein Tyrosine Phosphatases, Non-Receptor
Animals, COS Cells, Cell Membrane, Cercopithecus aethiops, Mice, Muscle, Skeletal, Myopathies, Structural, Congenital, Nerve Tissue Proteins, Phosphoric Monoester Hydrolases, Protein Binding, Protein Tyrosine Phosphatases, Non-Receptor
EMBO Rep.
Date: Oct. 01, 2013
PubMed ID: 23917616
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