Microtubules are essential to eukaryotic cytoskeletal structures, vesicular transportation, and mitosis. It consists mainly of two soluble protein subunits, alpha- and beta-tubulin. Alpha-tubulin binds to beta-tubulin to form a heterodimer that is subject to post-translation modifications (1). The tubulin dimer complex binds to GTP and assembles onto the positive ends of microtubules. After incorporation into the microtubules, bound GTP is hydrolyzed by beta-tubulin, but not alpha-tubulin. The stability of the dimer in the microtubules is dependent on the presence of beta-tubulin, since the dimer with GTP bound beta-tubulin is stable in microtubule integration (2). For both types of tubulins, the carboxy-terminal tail is post-translationally modified to regulate associated protein binding at the microtubule surface (3). Defects in alpha-tubulin are the cause of lissencephaly type 3 (LIS3), characterized by agyria (4).
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