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β-tubulin is a core cytoskeletal protein that, together with α-tubulin, forms dimers which polymerize to make microtubules—essential for maintaining cell structure, enabling mitosis, intracellular transport, and cell polarity. In its polymerized microtubule form, β-tubulin is a primary drug target for anti-cancer agents which either stabilize microtubules (preventing cell division) or destabilize them (causing failure of division and cell death). The protein’s functional diversity is controlled by isotype expression, post-translational modifications (like acetylation), and interaction with microtubule-associated proteins. Mutations, drug interactions, and altered expression are implicated in cancer, neurological disorders, and other diseases.
Stabilization of microtubules (e.g., paclitaxel binds β-tubulin in polymer to stop depolymerization, “freezing” microtubules and arresting mitosis); Destabilization of microtubules (e.g., vinca alkaloids and colchicine bind β-tubulin to inhibit polymerization, causing microtubule breakdown, mitotic arrest); Interference with dynamic instability (altering balance of growth/shrinkage); Some drugs block β-tubulin at specific sites and prevent or force conformational changes required for polymerization
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