The myotubularin–amphiphysin 2 complex in membrane tubulation and centronuclear myopathies
B Royer, K Hnia, C Gavriilidis, H Tronchère, V Tosch… - EMBO …, 2013 - embopress.org
B Royer, K Hnia, C Gavriilidis, H Tronchère, V Tosch, J Laporte
EMBO reports, 2013•embopress.orgMyotubularin (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 …
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 …
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.
embopress.org