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Abelson phosphorylation of CLASP2 modulates its association with microtubules and actin

机译：CLASP2的Abelson磷酸化调节其与微管和肌动蛋白的缔合

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摘要

The Abelson (Abl) non-receptor tyrosine kinase regulates the cytoskeleton during multiple stages of neural development, from neurulation, to the articulation of axons and dendrites, to synapse formation and maintenance. We previously showed that Abl is genetically linked to the microtubule (MT) plus end tracking protein (+TIP) CLASP in Drosophila. Here we show in vertebrate cells that Abl binds to CLASP and phosphorylates it in response to serum or PDGF stimulation. In vitro, Abl phosphorylates CLASP with a Km of 1.89 μM, indicating that CLASP is a bona fide substrate. Abl-phosphorylated tyrosine residues that we detect in CLASP by mass spectrometry lie within previously mapped F-actin and MT plus end interaction domains. Using purified proteins, we find that Abl phosphorylation modulates direct binding between purified CLASP2 with both MTs and actin. Consistent with these observations, Abl-induced phosphorylation of CLASP2 modulates its localization as well as the distribution of F-actin structures in spinal cord growth cones. Our data suggest that the functional relationship between Abl and CLASP2 is conserved and provides a means to control the CLASP2 association with the cytoskeleton.
机译：Abelson（Abl）非受体酪氨酸激酶在神经发育的多个阶段调节细胞骨架，从神经发育到轴突和树突的接合，再到突触的形成和维持。我们以前表明，Abl与果蝇中的微管（MT）加末端追踪蛋白（+ TIP）CLASP遗传相连。在这里，我们在脊椎动物细胞中显示Abl结合CLASP并使其磷酸化，以响应血清或PDGF刺激。在体外，Abl使CLASP的Km为1.89μM磷酸化，表明CLASP是真正的底物。我们通过质谱法在CLASP中检测到的Abl磷酸化酪氨酸残基位于先前定位的F-肌动蛋白和MT加末端相互作用域内。使用纯化的蛋白，我们发现Abl磷酸化调节纯化的CLASP2与MT和肌动蛋白之间的直接结合。与这些观察结果一致，Abl诱导的CLASP2磷酸化调节其定位以及F-肌动蛋白结构在脊髓视锥细胞中的分布。我们的数据表明Abl和CLASP2之间的功能关系是保守的，并提供了一种手段来控制CLASP2与细胞骨架的关联。

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