Myosin VI regulates actin structure specialization through conserved cargo-binding domain sites.

Myosin VI regulates actin structure specialization through conserved cargo-binding domain sites.
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DOI:
10.1371/journal.pone.0022755
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发表时间:
2011
期刊:
影响因子:
3.7
通讯作者:
Miller KG
Miller KG
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Isaji M;Lenartowska M;Noguchi T;Frank DJ;Miller KG

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Actin structures are often stable, remaining unchanged in organization for the lifetime of a differentiated cell. Little is known about stable actin structure formation, organization, or maintenance. During Drosophila spermatid individualization, long-lived actin cones mediate cellular remodeling. Myosin VI is necessary for building the dense meshwork at the cones' fronts. We test several ideas for myosin VI's mechanism of action using domain deletions or site-specific mutations of myosin VI. The head (motor) and globular tail (cargo-binding) domains were both needed for localization at the cone front and dense meshwork formation. Several conserved partner-binding sites in the globular tail previously identified in vertebrate myosin VI were critical for function in cones. Localization and promotion of proper actin organization were separable properties of myosin VI. A vertebrate myosin VI was able to localize and function, indicating that functional properties are conserved. Our data eliminate several models for myosin VI's mechanism of action and suggest its role is controlling organization and action of actin assembly regulators through interactions at conserved sites. The Drosophila orthologues of interaction partners previously identified for vertebrate myosin VI are likely not required, indicating novel partners mediate this effect. These data demonstrate that generating an organized and functional actin structure in this cell requires multiple activities coordinated by myosin VI.
在生长因子刺激后,肌球蛋白VI在高尔基体复合物和成纤维细胞的前缘及其磷酸化和募集到A431细胞的膜褶皱中的定位。
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