CCDC148 Inhibitors

Chemical inhibitors of CCDC148 exploit various molecular pathways to reduce the protein's activity. Staurosporine, a broad-spectrum protein kinase inhibitor, can impede the phosphorylation of numerous proteins, including CCDC148. By inhibiting the kinases that phosphorylate CCDC148, Staurosporine can decrease the protein's activity. Similarly, Palbociclib, by targeting CDK4 and CDK6, can disrupt cell cycle-regulated processes that involve CCDC148, leading to its inactivity. Trichostatin A, which inhibits histone deacetylases, can also affect CCDC148 if its function is regulated by acetylation; the hyperacetylated state maintained by Trichostatin A can suppress the protein's function. Another inhibitor, MG-132, targets the proteasome, leading to the build-up of ubiquitinated proteins, which may include CCDC148. This build-up can impede CCDC148's function due to the accumulation of malformed or aggregated proteins.

Further, LY294002, by inhibiting PI3K, can shut down signaling pathways that involve CCDC148, leading to a decrease in the protein's activity. Rapamycin, an mTOR inhibitor, can similarly affect CCDC148 if it is involved in mTOR-related cellular processes. The inhibition of mTOR can suppress CCDC148's role in cell growth and metabolism. In the context of MAP kinase pathways, SB203580 and PD98059 can attenuate CCDC148's activity by inhibiting p38 MAPK and MEK, respectively. SB203580 directly inhibits p38 MAPK, which may regulate CCDC148, while PD98059 blocks MEK, thereby disrupting the MAPK/ERK pathway which can regulate CCDC148's function. Additionally, PP2, an Src family kinase inhibitor, and Gefitinib, an EGFR tyrosine kinase inhibitor, can reduce the activity of CCDC148 if it is regulated by Src family kinase or EGFR signaling. Lastly, Y-27632, a ROCK inhibitor, can decrease CCDC148's activity if it is involved in pathways governed by Rho-associated kinases, by inhibiting these kinases and the pathways they control.