Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement?
Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement?
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DOI：
10.1126/science.1108408
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发表时间：
2005-06-03
期刊：
影响因子：
56.9
通讯作者：
Selvin, PR
中科院分区：
文献类型：
--
作者：
Kural, C;Kim, H;Selvin, PR
我们使用一纳米精度的荧光成像(FIONA)来分析细胞器在细胞中由传统的动蛋白和细胞质动力蛋白所做的运动。我们在培养的果蝇S2细胞中定位了一个绿色荧光蛋白(GFP)标记的过氧化物酶体，在1.1毫秒内达到1.5纳米以内，时间分辨率提高了400倍，足以确定动力蛋白和动力蛋白的平均步长类似于8纳米。此外，我们还发现，在体内，动力蛋白和动蛋白在过氧化物酶的转运过程中并不相互作用。相反，多个动蛋白或多个动力蛋白协同工作，产生的速度高达体外速度的10倍。
We used fluorescence imaging with one nanometer accuracy (FIONA) to analyze organelle movement by conventional kinesin and cytoplasmic dynein in a cell. We located a green fluorescence protein (GFP)-tagged peroxisome in cultured Drosophila S2 cells to within 1.5 nanometers in 1.1 milliseconds, a 400-fold improvement in temporal resolution, sufficient to, determine the average step size to be similar to 8 nanometers for both dynein and kinesin. Furthermore, we found that dynein and kinesin do not work against each other in vivo during peroxisome transport. Rather, multiple kinesins or multiple dyneins work together, producing up to 10 times the in vitro speed.