AI Article Synopsis
- The γ-tubulin ring complex (γTuRC) is essential for microtubule formation in cells, but how it works and is regulated remains unclear.
- Researchers developed a new microscopy technique to closely study how γTuRC interacts with tubulin and regulators on specially coated glass slides.
- This approach allows for real-time observation of microtubule nucleation at the single molecule level, providing insights into the dynamics and regulation of γTuRC.
Article Abstract
The γ-tubulin ring complex (γTuRC) is the major microtubule nucleator in cells. How γTuRC nucleates microtubules, and how nucleation is regulated is not understood. To gain an understanding of γTuRC activity and regulation at the molecular level, it is important to measure quantitatively how γTuRC interacts with tubulin and potential regulators in space and time. Here, we describe a total internal reflection fluorescence microscopy-based assay on chemically functionalized glass slides for the in vitro study of surface immobilized purified γTuRC. The assay allows to measure microtubule nucleation by γTuRC in real time and at a single molecule level over a wide variety of assay conditions, in the absence and presence of potential regulators. This setup provides a previously unavailable opportunity for quantitative studies of the kinetics of microtubule nucleation by γTuRC.
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| http://dx.doi.org/10.1007/978-1-0716-1983-4_21 | DOI Listing |
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