Tubulin protein

Tubulin is a globular cytoskeletal protein that exists primarily as alpha-tubulin and beta-tubulin subunits. These subunits form heterodimers that polymerize to create microtubules—hollow cylindrical structures essential for cell division, intracellular transport, maintenance of cell shape, and cellular motility. Drugs that bind tubulin and inhibit its ability to polymerize into microtubules disrupt the mitotic spindle formation required for chromosome segregation during mitosis. This mechanism is exploited in cancer therapy by agents such as colchicine and vinca alkaloids (vincristine, vinblastine), which arrest rapidly dividing cells in metaphase by destabilizing the microtubule network[1][2]. **Note:** The target name "Tubulin protein binding inhibiting microtubule polymerization" describes a mechanism rather than a canonical molecular entity or receptor. The correct target is "Tubulin protein," specifically referring to the alpha/beta tubulin dimer involved in microtubule dynamics. Therefore, this entry is marked as **is_incorrect = true** because it does not conform to standard naming conventions for molecular targets; it conflates the molecule with its pharmacological inhibition mechanism rather than specifying just the molecule itself[1][2].

Other names

Alpha-tubulinBeta-tubulinMicrotubule proteinTubulin dimer

Inhibition of microtubule polymerization by binding to tubulin dimers, preventing their assembly into microtubules[1][2]