| Drug | Effect | Mode of Action |
| Cytochalasin D | Actin filaments L | Binds + ends of actin filaments and prevents elongation. Membrane permeable. |
| Latrunculin | Actin filaments L | Binds G actin monomers and prevents them from polymerizing into filaments. Membrane permeable. |
| Phalloidin | Actin filaments J | Binds tightly all along the sides of actin filaments and stabilizes them against depolymerization. Not membrane permeable. |
| Jasplakinolide | Actin filaments J | Similar to phalloidin, but membrane-permeable. Induces actin polymerization by stimulating actin filament nucleation; stabilizes F-actin. See M. Bubb papers. |
| BDM (2,3-butanedione monoxime) | Myosin L | Inhibits myosin ATPases without affecting actin filaments. |
| Nocodazole | Microtubules L | Causes microtubules to depolymerize to tubulin subunits. |
| Colchicine | Microtubules
J and L |
Low concentration: blocks microtubule ends and prevents depolymerization. High Concentration: binds and sequesters free tubulin. Not readily reversible. |
| Taxol | Microtubules J | Binds to and stabilizes microtubules, preventing their depolymerization. High concentrations induce polymerization. |
| Vinblastine sulphate | Microtubules L | Binds b-tubulin to prevent polymerization. |
| Vincristine sulphate | Microtubules L | Binds free tubulin to prevent polymerization |
| Colcemid | Microtubules L | Binds and sequesters free tubulin. Readily reversible. |
| Low temperature | Microtubules L | Pushes microtubule-tubulin equilibrium away from polymerization. |
| Monastrol | Kinesin L | Mitosis inhibitor that does not interact with tubulin directly. Arrests cells in mitosis and specifically inhibits the motility of the mitotic kinesin, Eg5, a motor protein required for mitotic spindle formation and maintenance. |
Key:
L =
destabilizing/inactivating
effect
J =
stabilizing/activating
effect