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The Tubulin protein family comprises a group of evolutionarily conserved globular proteins that form heterodimers—primarily α-, β-, γ-, δ-, ε-, and ζ-tubilin—which assemble into linear protofilaments. These protofilaments associate laterally to form cylindrical structures known as microtubules, which are a major component of the eukaryotic cytoskeleton. Microtubes play critical roles in maintaining cell shape, enabling intracellular transport via motor proteins, forming cilia/flagella for motility, and orchestrating chromosome segregation during mitosis/meiosis. Tubulins possess intrinsic GTPase activity essential for their dynamic assembly/disassembly cycles. The disruption of these dynamics underlies both physiological processes like cell division and pathological states such as cancer proliferation—making them key targets for several classes of chemotherapeutic agents that either stabilize or destabilize microtube formation.[1][2][5]
Drugs targeting tubulins generally act by: - Inhibiting tubulin polymerization or depolymerization. - Disrupting microtubule dynamics required for mitosis/cell division. This leads to mitotic arrest and apoptosis in rapidly dividing cells such as cancer cells[1].
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