C17orf55 Inhibitors

Chemical inhibitors of C17orf55 disrupt the protein's function by targeting various aspects of the cell division cycle, particularly microtubule dynamics and spindle apparatus formation. Paclitaxel and vinblastine interfere with microtubule function, which is an integral part of cell division. Paclitaxel achieves this by stabilizing microtubules, preventing their disassembly and thus hindering the formation of the mitotic spindle. Vinblastine, on the other hand, binds to tubulin, the building block of microtubules, and inhibits their assembly. This action results in the inhibition of mitotic spindle function, which is necessary for successful cell division. Similarly, colchicine and podophyllotoxin target tubulin, with colchicine binding to tubulin and inhibiting polymerization, thereby preventing microtubule formation, while podophyllotoxin prevents the polymerization of tubulin as well, disrupting the formation of microtubules.

Monastrol and S-Trityl-L-cysteine focus on the inhibition of the kinesin Eg5, a motor protein that is essential for the separation of centrosomes and the bipolar spindle formation. Monastrol specifically inhibits the function of Eg5, leading to the formation of monopolar spindles, which are ineffective in cell division. S-Trityl-L-cysteine also inhibits Eg5, reinforcing the inhibition of the mitotic spindle apparatus. Nocodazole contributes to this disruption by depolymerizing microtubules, leading to the disintegration of the microtubule network essential for mitosis. Alisertib, ZM 447439, and BI 2536 take a slightly different approach by inhibiting essential kinases involved in cell cycle progression. Alisertib inhibits Aurora A kinase, which is crucial for mitotic entry and spindle assembly, while ZM 447439 inhibits Aurora kinase, affecting cytokinesis and chromosome alignment. BI 2536 inhibits polo-like kinase 1 (PLK1), which affects spindle formation and checkpoint regulation. Purvalanol A targets cyclin-dependent kinases that are essential for the progression of the cell cycle. By inhibiting these kinases, Purvalanol A halts the cell cycle. Lastly, SP600125 inhibits the Jun N-terminal kinase (JNK), which impacts cell cycle progression and the cell's ability to undergo division, thus indirectly affecting the role of C17orf55 in these processes. Each of these chemical inhibitors, through their unique mechanisms, can disrupt the normal functioning of C17orf55, which plays a role in cell cycle progression and mitosis.