Tubulin (microtubule protein)

The target described as "Microtubule polymerization inhibition by vincristine" refers to the interaction of the drug vincristine with tubulin, the primary structural protein of microtubules. Vincristine binds specifically to the β-tubulin subunit, inhibiting its polymerization into microtubules that are critical for the mitotic spindle and diverse cellular functions including cell division, intracellular trafficking, and maintenance of cell shape. Disruption of microtubule dynamics by vincristine leads to arrest of the cell cycle in metaphase, ultimately inducing apoptosis, particularly in rapidly dividing cells like cancer cells. While "microtubule polymerization inhibition by vincristine" is a pharmacological effect, the true molecular therapeutic target is tubulin (the microtubule). Vincristine and other microtubule-targeting agents play a central role in cancer therapy but are associated with significant toxicities, especially neurotoxicity and myelosuppression[1][2][3][5][7]. Note: The phrase "Microtubule polymerization inhibition by vincristine" does not refer to a specific molecule or receptor but rather describes a pharmacological mechanism. The canonical molecular target for this mechanism is tubulin, specifically the β-tubulin subunit. Therefore, the entry should be marked as is_incorrect: true due to lack of precise target nomenclature; the correct form should be "Tubulin (β-tubulin)" or simply "Tubulin".

Other names

MicrotubuleTubulin proteinTubulin dimerβ-tubulinα/β-tubulinMicrotubule network

Inhibition of tubulin polymerization into microtubules; Disruption of mitotic spindle formation; M-phase cell cycle arrest (metaphase block); Induction of apoptosis in rapidly dividing cells; Disruption of intracellular signaling pathways (e.g., AKT/mTOR inhibition)[1][2][3][7]