Interactions between the Microtubule Binding Protein EB1 and F-Actin.
Interactions between the Microtubule Binding Protein EB1 and F-Actin.
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DOI：
10.1016/j.jmb.2016.01.032
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发表时间：
2016-03-27
影响因子：
5.6
通讯作者：
Goodson HV
中科院分区：
文献类型：
--
作者：
Alberico EO;Zhu ZC;Wu YO;Gardner MK;Kovar DR;Goodson HV
许多细胞过程包括细胞分裂和细胞迁移需要肌动蛋白和微管（MT）细胞骨架之间的协调。这种协调机制目前尚不清楚，但已知蛋白质如formin和IQGAP 1参与其中。我们发现，MT结合蛋白EB 1（末端结合蛋白1），MT动力学的关键调节器，可以直接结合到丝状肌动蛋白（F-肌动蛋白）F-肌动蛋白。我们确定，EB 1：F-肌动蛋白相互作用是盐敏感性和生理盐浓度下弱，但可能是相关的背景下，局部浓度的肌动蛋白是高的。使用生物信息学和诱变，我们发现，EB 1：F-肌动蛋白结合位点部分重叠的特征EB 1：MT结合界面。相应地，竞争实验表明EB 1可以结合F-肌动蛋白或MT，但不能同时结合两者。这些观察结果表明，EB 1：F-肌动蛋白的相互作用可能会负调节EB 1：MT的相互作用，我们推测，这种相互作用可能有助于细胞差异调节MT的稳定性，在肌动蛋白丰富的皮层，而不是细胞内部。
Many cellular processes including cell division and cell migration require coordination between the actin and microtubule (MT) cytoskeletons. This coordination is as-yet poorly understood, but proteins such as formins and IQGAP1 are known to be involved. We show that the MT binding protein EB1 (end-binding protein 1), a key regulator of MT dynamics, can bind directly to filamentous actin (F-actin) F-actin. We determined that the EB1:F-actin interaction is salt sensitive and weak under physiological salt concentrations but might be relevant in contexts where the local concentration of actin is high. Using bioinformatics and mutagenesis, we found that the EB1:F-actin binding site partially overlaps the well-characterized EB1:MT binding interface. Congruently, competition experiments indicate that EB1 can bind to F-actin or MTs but not both simultaneously. These observations suggest that EB1:F-actin interactions may negatively regulate EB1:MT interactions, and we speculate that this interaction may assist cells in differentially regulating MT stability in the actin-rich cortex as opposed to the cell interior.