Microtubule polymerization in neutrophils

Microtubule polymerization in neutrophils is the dynamic assembly of α- and β-tubulin heterodimers to form microtubules, which are essential for establishing neutrophil polarity, regulating migration (chemotaxis), and supporting effector functions such as phagocytosis and nuclear dynamics[1][2][3][5][6]. In response to chemokine stimulation, neutrophils rapidly elongate their microtubule network, facilitating intracellular transport and spatial polarization in preparation for migration towards inflammatory signals. Disruption or pharmacological modulation of microtubule polymerization impairs neutrophil chemotaxis and can influence immune defense, which is relevant both for host immunity and as a target of specific cancer chemotherapies (taxanes, vinca alkaloids, colchicine)[5][7]. However, as a "target," microtubule polymerization describes a process rather than a single druggable protein; drugs act primarily by binding to tubulin subunits, affecting microtubule dynamics systemically.

Other names

Microtubule assemblyTubulin polymerizationMT polymerization

Microtubule stabilization (e.g., Paclitaxel/Taxol binds and stabilizes microtubules, suppressing their dynamics); Microtubule depolymerization (e.g., Nocodazole, Colchicine inhibit polymerization, cause disassembly)