Microtubule (Eribulin-binding site) (null)

Microtubules are tubular polymers composed of α- and β-tubulin heterodimers, forming key components of the eukaryotic cytoskeleton. They are essential for mitosis, intracellular transport, and cell structure maintenance. Eribulin is a synthetic analog of halichondrin B and acts as a microtubule dynamics inhibitor: it binds predominantly at the plus ends of microtubules, inhibiting further polymerization without affecting shortening, and sequesters tubulin into aggregates unable to assemble functional microtubules. This leads to cell cycle arrest at G2/M, mitotic spindle disruption, and apoptotic cell death. Unlike other microtubule-targeting agents, eribulin does not affect the rate of microtubule shortening and displays unique effects on the tumor microenvironment, such as vascular remodeling and suppression of epithelial-mesenchymal transition[1][2][3][5][6][7].

Other names

TubulinMicrotubuleβ-tubulinMicrotubule polymerMicrotubule cytoskeleton

- Inhibition of microtubule polymerization (prevents microtubule growth at the plus end) - Sequestration of tubulin into nonproductive aggregates - Disruption of mitotic spindle formation - Induction of mitotic arrest and apoptosis due to prolonged mitotic blockage - Distinct from vinca alkaloids (not significantly affecting microtubule shortening/dynamics) - May alter tumor microenvironment, promoting vascular remodeling and reduced hypoxia (eribulin-specific) - Opposes epithelial-mesenchymal transition (EMT); promotes epithelial state (eribulin-specific)