Fluorescence imaging of GFP-tagged peroxisomes in Drosophila cells revealed an average step size of ~8 nm for both dynein and kinesin, which work together to produce up to 10 times the in vitro speed.
In vivo, multiple kinesins or dyneins work cooperatively to transport peroxisomes, achieving speeds up to 10 times faster than in vitro without working against each other.
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 approximately 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.
Kural et al. (Thu,) reported a other. Fluorescence imaging with one nanometer accuracy (FIONA) was evaluated on Average step size and coordination of dynein and kinesin during peroxisome transport. Fluorescence imaging of GFP-tagged peroxisomes in Drosophila cells revealed an average step size of ~8 nm for both dynein and kinesin, which work together to produce up to 10 times the in vitro speed.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: