Competition and compensation: dissecting the biophysical and functional differences between the class 3 myosin paralogs, myosins 3a and 3b.
Competition and compensation: dissecting the biophysical and functional differences between the class 3 myosin paralogs, myosins 3a and 3b.
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DOI：
10.4161/bioa.21733
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发表时间：
2012-09
期刊：
影响因子：
--
通讯作者：
Gov NS
中科院分区：
文献类型：
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作者：
Manor U;Grati M;Yengo CM;Kachar B;Gov NS
静纤毛是肌动蛋白突起，具有非常明确的长度和组织。最近的一系列论文报道了多种肌球蛋白马达蛋白参与调节静纤毛结构，通过将肌动蛋白调节货物运输到静纤毛的尖端。1 -13在我们最近的论文中，我们表明两种旁系同源的3类肌球蛋白-Myo 3a和Myo 3b-都以非常相似的方式将肌动蛋白调节蛋白Espin 1（Esp 1）运输到静纤毛和丝状伪足尖端，虽然不相同的时尚。1在这里，我们提出的实验和计算数据表明，这两种蛋白质的生物物理和生物化学性质之间的细微差异可以帮助我们了解这些肌球蛋白物种如何靶向和调节肌动蛋白突起的长度。
Stereocilia are actin protrusions with remarkably well-defined lengths and organization. A flurry of recent papers has reported multiple myosin motor proteins involved in regulating stereocilia structures by transporting actin-regulatory cargo to the tips of stereocilia.1-13 In our recent paper, we show that two paralogous class 3 myosins — Myo3a and Myo3b — both transport the actin-regulatory protein Espin 1 (Esp1) to stereocilia and filopodia tips in a remarkably similar, albeit non-identical fashion.1 Here we present experimental and computational data that suggests that subtle differences between these two proteins’ biophysical and biochemical properties can help us understand how these myosin species target and regulate the lengths of actin protrusions.