【摘 要】
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Objective Typical mature neurons usually have highly polarized structure.The polarization of axon and dendrites underlies the unidirectional flow of information transfer, which is essential for the es
【机 构】
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Laboratory of Neural Plasticity, Institute of Genetics and Cytology, Northeast Normal University, Ch
【出 处】
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中国神经科学学会第九届全国学术会议暨第五届会员代表大会
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Objective Typical mature neurons usually have highly polarized structure.The polarization of axon and dendrites underlies the unidirectional flow of information transfer, which is essential for the establishment of functional circuits in the central nervous system.Neuronal polarization depends on cytoskeleton reorganization.Myosin X (Myo X), a vertebrate-specific unconventional myosin, is not only capable of binding actin and microtubule, but also interacting with cytoskeleton regulators, such as PIP3 and Mena/VASP.In this study, we engaged in studying the potential role of Myo X in neuronal polarization.Methods The primarily culture system of dissociated rodent hippocampal neurons together with electroporation is applied to loss-of-function analysis.We then analyzed stable and dynamic microtubules in Myo X-suppressed neurons by staining for acetylated and tyrosinated α-tubulin.To dissect the molecular mechanism underlying Myo X-mediated axon specification, we constructed series of truncated mutations and tested their effect on neuronal polarization.Rescued experiments were performed by cotransfecting Pll0, RaplBvl2 or Cdc42L28 with Myo X siRNA.Wd-Cdc42 and Myo X siRNA or scramble siRNA were cotransfected into NIH 3T3 cells and pull-down assay was performed to test Cdc42-GTP.Results Suppressing the expression of Myo X inhibited axon formation and the majority of Myo X-suppressed neurons arrested in stage 2.However, microtubule stabilization in one neurite was still higher than others suggesting that Myo X functioned in axon outgrowth and specification.In addition, in respect that cytochalasin D rescued the polarity defect caused by Myo X knockdown, we presume that Myo X participate in neuronal polarization via actin signaling pathway.Myo X acted downstream of PI3K through PH domain in a motor-independent way.Cdc42L28 rescued the loss of polarity caused by Myo X siRNA and pull-down assay revealed that Myo X siRNA suppressed Cdc42 activation.Conclusion Myo X regulates Cdc42 activity downstream of PI3K in neuronal polarization.
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