Tubulin alpha chain and Tubulin beta chain (heterodimer, microtubule subunits) (α-tubulin and β-tubulin)

Tubulin alpha and beta chains are highly conserved globular proteins that form obligate heterodimers, which polymerize to construct microtubules—a key component of the eukaryotic cytoskeleton involved in cell shape, intracellular transport, and mitosis[1][5][6][7][9]. Each monomer binds GTP; the α-tubulin nucleotide is nonexchangeable, while β-tubulin’s nucleotide can hydrolyze and exchange GTP, driving microtubule assembly dynamics[1][6][8]. Tubulin exists in multiple isotypes encoded by distinct genes and is subject to various post-translational modifications, contributing to cellular functions, neuronal development, and disease states[7][9]. Aberrations in tubulin structure, expression, or modification are implicated in cancer, neurodevelopmental disorders, and confer resistance to common chemotherapeutics that directly target microtubules[7][9]. Microtubule-targeting agents are a mainstay in chemotherapy but are limited by side effects and acquired resistance in tumors[7].

Other names

Tubulin alpha-1A chain (TUBA1A)Tubulin beta chainAlpha-tubulinBeta-tubulinTubulin heterodimerMicrotubule protein

Inhibition of microtubule polymerization (e.g., vincristine, colchicine); Stabilization of microtubules (e.g., paclitaxel, docetaxel); Disruption of mitotic spindle and cell division; Antimicrotubule agent (prevents dynamic instability required for mitosis)