Tubulin biochemistry confers intrinsic differences in microtubule dynamics and drug sensitivity between species | New Voices in Infection Biology

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Talk abstract:

In almost every eukaryotic cell, reproduction and function are dependent on the small protein tubulin, which assembles into microtubules. ‘Tubulin’, however, is not a single protein but rather a complex mixture of different tubulin isoforms with varying post-translational modifications (PTMs). Cells express different tubulin genes, encoding distinct isoforms. The combination of different isoforms together with multiple PTMs gives rise to a staggering complexity of a cell’s tubulin proteome. How microtubule dynamics and tubulin druggability are affected by these different biochemical characteristics remains unknown. We have recently developed a method that allows for the purification of physiologically relevant tubulin from any eukaryotic cell or tissue type. This has opened the door for interrogating how the tubulin molecule has evolved to confer intrinsic differences in microtubules between species. I will talk about how differences in tubulin biochemistry (1) can control spindle size in frogs and (2) effect drug sensitivity between Plasmodium falciparum and its human host.