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Isolation of intraflagellar transport trains.

Mencarelli C, Mitchell A, Leoncini R, Rosenbaum J, Lupetti P - Cytoskeleton (Hoboken) (2013)

Bottom Line: Moreover, the particles forming isolated IFT trains are structurally similar to the individual particles found in the ∼17S gradient peak.Our results provide the first direct evidence that ∼17S particles do indeed compose the IFT trains.The paper also represents the first isolation of the IFT trains, and opens new possibilities for higher resolution studies on their structure and how particles are attached to each other to form the particle trains.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.

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A. Isolated strings of particles are specifically labeled by IFT antibodies. Gold particles have been indicated in this figure by arrowheads, without any distinction between complex A and complex B labeling. B. Both complex A (white arrows: IFT139, 5-nm gold) and complex B (black arrows: IFT46, 10-nm gold) antibodies react with IFT particle arrays. Brackets in both Figs. A and B indicate regions where particles are arranged in a double row.
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fig05: A. Isolated strings of particles are specifically labeled by IFT antibodies. Gold particles have been indicated in this figure by arrowheads, without any distinction between complex A and complex B labeling. B. Both complex A (white arrows: IFT139, 5-nm gold) and complex B (black arrows: IFT46, 10-nm gold) antibodies react with IFT particle arrays. Brackets in both Figs. A and B indicate regions where particles are arranged in a double row.

Mentions: IFT immunolabeling was specifically associated with the arrays of particles in the gradient pellet (Fig. 5A). When observed at a higher magnification, strings of particles appear to be labeled by both IFT139 (white arrows in Fig. 5B) and IFT46 (black arrows in Fig. 5B) antibodies. This finding clearly indicates that both complex A and complex B are present in the same string of particles.


Isolation of intraflagellar transport trains.

Mencarelli C, Mitchell A, Leoncini R, Rosenbaum J, Lupetti P - Cytoskeleton (Hoboken) (2013)

A. Isolated strings of particles are specifically labeled by IFT antibodies. Gold particles have been indicated in this figure by arrowheads, without any distinction between complex A and complex B labeling. B. Both complex A (white arrows: IFT139, 5-nm gold) and complex B (black arrows: IFT46, 10-nm gold) antibodies react with IFT particle arrays. Brackets in both Figs. A and B indicate regions where particles are arranged in a double row.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4060975&req=5

fig05: A. Isolated strings of particles are specifically labeled by IFT antibodies. Gold particles have been indicated in this figure by arrowheads, without any distinction between complex A and complex B labeling. B. Both complex A (white arrows: IFT139, 5-nm gold) and complex B (black arrows: IFT46, 10-nm gold) antibodies react with IFT particle arrays. Brackets in both Figs. A and B indicate regions where particles are arranged in a double row.
Mentions: IFT immunolabeling was specifically associated with the arrays of particles in the gradient pellet (Fig. 5A). When observed at a higher magnification, strings of particles appear to be labeled by both IFT139 (white arrows in Fig. 5B) and IFT46 (black arrows in Fig. 5B) antibodies. This finding clearly indicates that both complex A and complex B are present in the same string of particles.

Bottom Line: Moreover, the particles forming isolated IFT trains are structurally similar to the individual particles found in the ∼17S gradient peak.Our results provide the first direct evidence that ∼17S particles do indeed compose the IFT trains.The paper also represents the first isolation of the IFT trains, and opens new possibilities for higher resolution studies on their structure and how particles are attached to each other to form the particle trains.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.

Show MeSH
Related in: MedlinePlus