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Kinesin and Dynein-Dynactin at Intersecting Microtubules: Motor Density Affects Dynein Function

机译:驱动蛋白和动力蛋白-动力蛋白在相交的微管:运动密度影响动力蛋白功能。

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摘要

Kinesin and cytoplasmic dynein are microtubule-based motor proteins that actively transport material throughout the cell. Microtubules can intersect at a variety of angles both near the nucleus and at the cell periphery, and the behavior of molecular motors at these intersections has implications for long-range transport efficiency and accuracy. To test motor function at microtubule intersections, crossovers were arranged in vitro using flow to orient successive layers of filaments. Single kinesin and cytoplasmic dynein-dynactin molecules fused with green-fluorescent protein, and artificial bead cargos decorated with multiple motors, were observed while they encountered intersections. Single kinesins tend to cross intersecting microtubules, whereas single dynein-dynactins have a more varied response. For bead cargos, kinesin motion is independent of motor number. Dynein beads with high motor numbers pause, but their actions become more varied as the motor number decreases. These results suggest that regulating the number of active dynein molecules could change a motile cargo into one that is anchored at an intersection, consistent with dynein's proposed transport and tethering functions in the cell.
机译:驱动蛋白和细胞质动力蛋白是基于微管的运动蛋白,可在整个细胞中主动转运物质。微管可以在细胞核附近和细胞外围以各种角度相交,并且分子电动机在这些相交处的行为对长距离传输效率和准确性具有影响。为了测试微管相交处的运动功能,在体外使用流动排列交叉以定向连续的细丝层。当观察到相交点时,观察到与绿色荧光蛋白融合的单驱动蛋白和细胞质动力蛋白-动力蛋白分子,以及装饰有多个马达的人造珠货物。单个驱动蛋白趋于穿过相交的微管,而单个动力蛋白-动力蛋白具有更多变化的响应。对于珠货物,驱动蛋白的运动与电机数无关。具有高运动数的达因珠悬浮,但随着运动数减少,它们的作用变得更加多样。这些结果表明,调节活性达因分子的数量可以将运动货物变成锚定在交叉点上的货物,这与达因在细胞中提出的转运和束缚功能相一致。

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