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arMS interacts with α-syntrophin: implications for the localization and signaling of EphA4 at the neuromuscular synapse

ARMS interacts with α-syntrophin: implications for the loca...

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中国神经科学学会第六届学术会议暨学会成立十周年庆祝大会

作者： k.ok.On. Lai Juan Carlos arévalo Stanley C. Froehner Marvin E. Adams Moses V. Chao Nancy Y. Ip Dept. of Biochemistry Hong k.ng Univ. of Science and Technology Sk.rball Institute of Biomolecular Medicine New York.Univ. Sch. of Med. New YorkNY 10016USA Dept. of Physiology ＆ Biophysics Univ. of Washington SeattleWA 98195 USA Dept. of Physiology ＆ Biophysics Univ. of Washington SeattleWA 98195 USA Sk.rball Institute of Biomolecular Medicine New York.Univ. Sch. of Med. New YorkNY 10016USA Dept. of Biochemistry Hong k.ng Univ. of Science and Technology

＜正＞Recent accumulating evidence suggests that both Eph and Trk.receptors play important roles at the neuromuscular junctions （NMJ）. The identification of arMS （ank.rin repeat-rich membrane spanning） as a novel substrate for these receptors prompted us to investigate the potential functions of arMS at the NMJ. In this study, we showed that arMS was expressed in developing muscle and became concentrated at the NMJ during the first postnatal week. Using yeast two-hybrid screening, we identified the PDZ domain protein α-syntrophin as an arMS-interacting partner in muscle. The expression profile of α-syntrophin in muscle was similar to that exhibited by arMS and EphA4. Interestingly, overexpression of α-syntrophin induced arMS clustering in a PDZ-dependent manner. Moreover, only α- and β2-syntrophins, but not β1 syntrophin, were able to interact with arMS and induce the formation of arMS clusters. In an attempt to identify other components of the arMS/syntrophin complex, we found that arMS associated with EphA4 and that this interaction resulted in an enhanced jak and Stat tyrosine phosphorylation, which was further augmented by α-Syntrophin in a PDZ-dependent manner. More importantly, tyrosine phosphorylation of EphA4 induced by ephrin-A1 was attenuated in C2C12 myotubes upon the inhibition of arMS and a-syntrophin expression by siRNA transfection. Finally, disrupted localization of arMS and EphA4 at the NMJ was observed in a-syntrophin null mice. Tak.n together, our findings suggest an important role of arMS in regulating postsynaptic signaling events through syntrophin-mediated localization of receptor tyrosine k.nases.

关键词： Eph receptor receptor tyrosine k.nase PDZ neuromuscular junction syntrophin

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