Reactivation of organelle movements along the cytoskeletal framework of a giant freshwater ameba
Reactivation of organelle movements along the cytoskeletal framework of a giant freshwater ameba
复制标题
沿着巨型淡水阿米巴细胞骨架的细胞器运动的重新激活
作者：
M. Koonce;M. Schliwa
巨大的淡水阿米巴Reticulomyxa的外周摄食网络可以很容易地和迅速地裂解，产生广泛的，稳定的，完全暴露的共线微管和微丝的细胞骨架框架。如果加入ATP，大多数仍然附着在这个框架上的细胞器以高达20微米/秒的速率恢复快速跳跃运动。这种裂解的模型系统也能够具有其他形式的运动性，即微管束的主动张开和大量流动。其他核苷三磷酸不会发生再活化，需要镁离子，对高浓度的β-9-（3-[2-羟基壬基]）腺嘌呤不敏感，仅在约100 μ M浓度下对钒酸盐敏感，在浓度大于100 μ M时被N-乙基马来酰亚胺抑制。这种重新激活的生理学表明细胞器运输电机不同的细胞质动力蛋白，可能是最近描述的驱动蛋白。该系统可以作为阐明细胞内运输机制的模型，此外，还提供了一个独特的机会来研究微管和微丝之间的关联。
The peripheral feeding network of the giant freshwater ameba Reticulomyxa can be easily and rapidly lysed to produce an extensive, stable, and completely exposed cytoskeletal framework of colinear microtubules and microfilaments. Most of the organelles that remain attached to this framework resume rapid saltatory movements at rates of up to 20 micron/s if ATP is added. This lysed model system is also capable of other forms of motility, namely an active splaying of microtubule bundles and bulk streaming. Reactivation does not occur with other nucleoside triphosphates, requires Mg ions, is insensitive to even high concentrations of erythro-9-(3-[2-hydroxynonyl]) adenine, is sensitive to vanadate only at concentrations of approximately 100 microM, and is inhibited by N-ethylmaleimide at concentrations greater than 100 microM. The physiology of this reactivation suggests an organelle transport motor distinct from cytoplasmic dynein and possibly the recently described kinesin. This system can serve as a model for elucidating the mechanisms of intracellular transport and, in addition, provides a unique opportunity to examine associations between microtubules and microfilaments.
计算机增强视频显微镜：可以实时生成经过数字处理的显微镜图像。
DOI：
10.1073/pnas.78.11.6927
发表时间：
1981
影响因子：
11.1
作者：
Walter,RJ;Berns,MW
通讯作者：
Berns,MW
钒酸盐诱导的动力蛋白 ATP 酶抑制的前稳态动力学分析。
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Shimizu,T;Johnson,KA
通讯作者：
Johnson,KA