Recently, I issued a post about a method which allows measuring microtuble binding capabilities of proteins of interest. Today, I invite you to look at methods for measuring the dynamic polymerisation of tubulin to microtubules and to detect the impact of compounds or other variables in your experiments on this process.
Tubulin represents one of the major cytoskeleton structures. It plays an important role in cell structure, intracellular transport, and mitosis. In eukaryotic cells, tubulin polymerizes to form structures called microtubules (MTs) (Fig. 1). When tubulin polymerizes it initially forms proto-filaments, MTs consist of 13 protofilaments and are 25nm in diameter, each um of MT length is composed of 1650 heterodimers. Microtubules are highly ordered fibers that have an intrinsic polarity, shown schematically in Figure 2. Tubulin can polymerize from both ends in vitro, however, the rate of polymerization is not equal. It has therefore become the convention to call the rapidly polymerizing end the plus-end of a microtubule and the slowly polymerizing end the minus-end. In vivo, the plus end of a microtubule is distal to the microtubule organizing center.