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首页> 外文期刊>Molecular cell >Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering
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Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering

机译：全长肌球蛋白VI在单体聚集后沿肌动蛋白丝二聚并逐步移动

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摘要

Myosin VI is a reverse direction actin-based motor capable of taking large steps (30-36 nm) when dimerized. However, all dimeric myosin VI molecules so far examined have included nonnative coiled-coil sequences, and reports on full-length myosin VI have failed to demonstrate the existence of dimers. Herein, we demonstrate that full-length myosin VI is capable of forming stable, processive dimers when monomers are clustered, which move up to 1-2 mu m in similar to 30 nm, hand-over-hand steps. Furthermore, we present data consistent with the monomers being prevented from dimerizing unless they are held in close proximity and that dimerization is somewhat inhibited by the cargo binding tail. A model thus emerges that cargo binding likely clusters and initiates dimerization of full-length myosin VI molecules. Although this mechanism has not been previously described for members of the myosin superfamily, it is somewhat analogous to the proposed mechanism of dimerization for the kinesin Unc104.
机译：Myosin VI是一种基于反向肌动蛋白的马达，二聚时能够采取较大的步幅（30-36 nm）。然而，到目前为止，所有检查的二聚肌球蛋白VI分子都包括非天然螺旋线圈序列，有关全长肌球蛋白VI的报道未能证明二聚体的存在。本文中，我们证明了全长肌球蛋白VI能够在单体成簇时形成稳定的连续二聚体，其以类似于30 nm的移交步骤移动至1-2μm。此外，我们提出的数据与单体不能二聚化一致，除非它们紧密靠近，并且二聚化在某种程度上受到货物束缚尾部的抑制。因此，出现了一个模型，表明货物结合可能会聚集并引发全长肌球蛋白VI分子的二聚化。尽管以前没有针对肌球蛋白超家族成员描述这种机制，但它与驱动蛋白Unc104的二聚化提议机制有些相似。

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