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首页> 外文期刊>Journal of Cellular Physiology >Characterization of a novel EB1 acetylation site important for the regulation of microtubule dynamics and cargo recruitment
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Characterization of a novel EB1 acetylation site important for the regulation of microtubule dynamics and cargo recruitment

机译：小说EB1乙酰化网站的描述对微管的规定很重要动力学和货物招聘

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摘要

Microtubule plus ends undergo highly dynamic modifications to regulate different aspects of cellular activities. Most microtubule plus‐end tracking proteins (+TIPs) are recruited to the microtubule ends by the master loading factor, end‐binding protein 1 (EB1). These proteins coordinately regulate microtubule dynamics and cellular plasticity. Acetylation is known to modulate EB1 function; however, the molecular details of EB1 acetylation remain largely unclear. We mapped the acetylation pattern of EB1 and identified several previously uncharacterized sites of EB1 acetylation. We examined the effects of lysine‐212 (K212) acetylation and found that acetylation of this site accelerates autophagy‐mediated EB1 degradation. By time‐lapse microscopy, we found that the acetylation‐deficient K212R mutant increased the percentage of fast‐growing and long‐lived microtubules. Although K212 acetylation did not affect microtubule stability in vitro and the association of EB1 with microtubules, the K212R mutant significantly promoted microtubule regrowth in cells. Coimmunoprecipitation assays further revealed that the K212 site was critical for the recruitment of different +TIP cargoes. These data thus uncover a critical role for a novel EB1 acetylation site in regulating the dynamic structure of microtubules.
机译：微管+经历高度动态的结束修改规范的不同方面细胞的活动。跟踪(+小费)招募到的蛋白质微管两端通过主加载因子,终端结合蛋白1 (EB1)。协调调节微管动力学和细胞的可塑性。调节EB1功能;EB1乙酰化作用仍然很大程度上的细节不清楚。和之前几无特征识别EB1乙酰化的网站。的赖氨酸量212 (K212)乙酰化作用,发现这个网站的乙酰化加速自噬介导EB1退化。显微镜,我们发现乙酰化作用量不足K212R变异增加了的比例快速增长和长期居住微管。在体外和影响微管稳定K212R EB1协会与微管变异显著促进微管在细胞再生。进一步表明K212网站是至关重要的不同的招聘+货物。这些数据从而揭示一个至关重要的作用小说在规范EB1乙酰化的网站微管的动态结构。

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