CEP68 Inhibitors

Chemical inhibitors of CEP68 can affect its function by targeting the microtubule network, which is essential for its role in centrosome cohesion and function. Peloruside A is such an inhibitor that stabilize microtubules, thus preventing their depolymerization. This stabilization indirectly inhibits CEP68 by altering the dynamic instability of microtubules, a critical aspect of microtubule function that CEP68 utilizes for maintaining centrosome integrity. On the other hand, Nocodazole and Colchicine take an opposite approach by binding to tubulin and inhibiting its polymerization into microtubules. This disruption hinders the proper organization of microtubules around the centrosomes, thereby indirectly inhibiting the function of CEP68, as it cannot maintain centrosome cohesion without an intact microtubule network. Further adding to the arsenal of CEP68 inhibitors, Vinblastine and Vincristine bind to tubulin as well, preventing microtubule assembly. This action indirectly impairs CEP68's ability to interact with microtubules, which is essential for its function in centrosome linkage. Similarly, Griseofulvin, Podophyllotoxin, and Parbendazole interfere with microtubule dynamics by preventing tubulin polymerization, thus disrupting the centrosomal microtubule array and indirectly inhibiting CEP68's role in centrosome cohesion. Eribulin inhibits the growth phase of microtubules, leading to destabilized microtubule structures and, as a result, indirectly inhibits CEP68. Noscapine alters microtubule dynamics without affecting polymerization, yet this change is enough to indirectly inhibit CEP68 as it affects the microtubule functions that are essential for CEP68's activity. Lastly, Monastrol specifically inhibits the kinesin Eg5, which is essential for spindle pole integrity during cell division. By disturbing the spindle assembly, Monastrol indirectly inhibits CEP68, as the protein relies on the proper function of spindle microtubules to maintain centrosome cohesion.