Molecular mechanisms for recognition of neuronal polarity by kinesin

神经元形成独特的轴突和树突隔间，这对定向信号传导很重要，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，酪氨酸微管蛋白是丰富的体树突阻止驱动蛋白1结合微管，从而调节极化驱动蛋白1运输到轴突。因此，抑制海马神经元中微管蛋白酪氨酸化会破坏神经元极性。我们的研究确定了区分轴突微管和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.