Molecular mechanisms for recognition of neuronal polarity by kinesin

神经元形成独特的轴突和树突间隔，这对定向信号很重要，但区分轴突和树突的机制仍然难以捉摸。在这项研究中，我们发现在躯体突中丰富的酪氨酸化微管蛋白阻止了Kinesin-1与微管的结合，从而调节了极化的Kinesin-1向轴突的运输。海马神经元中微管蛋白酪氨酸化的抑制一直扰乱神经元的极性。我们的研究发现了区分轴突微管和躯体树突微管的分子机制，并提供了参与神经元形态发生的新的分子机制。

Neurons form distinctive axonal and dendritic compartments that are important for directional signaling, but the mechanisms that discriminate axons from dendrites remain elusive. In this study, we found that tyrosinated tubulins that are abundant in somatodendrites prevent kinesin-1 from binding to microtubules, thereby regulate polarized kinesin-1 trafficking to the axon. Consistently, inhibition of tubulin tyrosination in hippocampal neurons disrupted neuronal polarity. Our study identifies a molecular mechanism that discriminates the axonal microtubules from somatodendritic microtubules, and provided novel molecular mechanisms involved in the neuronal morphogenesis.