TMEM117 Inhibitors

Chemical inhibitors of TMEM117 can impede the protein's function through a variety of mechanisms that target its association with cellular membranes or its role in signaling pathways. Phloretin disrupts TMEM117 by interfering with its interaction with cellular membranes, possibly altering the dynamics or the lipid composition essential for its proper localization or activity. Similarly, Chlorpromazine affects membrane integrity and fluidity, which could impair TMEM117's membrane-associated functions. Progesterone and Tamoxifen, through their interactions with membrane-bound proteins and the lipid environment, can alter the membrane association of TMEM117 or affect the microenvironment necessary for its functional conformation. Genistein inhibits TMEM117 by targeting protein tyrosine kinases, which may affect the phosphorylation status of TMEM117 or proteins in close interaction with it.

Verapamil and Diltiazem, both calcium channel blockers, inhibit TMEM117 by altering calcium homeostasis, a critical factor for the protein's role in calcium-dependent signaling pathways. Nifedipine, another agent in this class, also modulates calcium signaling, which is likely to affect TMEM117's function. Quinidine influences cellular excitability and signaling by inhibiting voltage-gated sodium channels, which can disrupt TMEM117 if it is functionally connected to sodium-dependent processes. Haloperidol, by disrupting dopamine signaling pathways, may indirectly affect TMEM117's role related to ion channel activity and membrane dynamics. Amiodarone alters the lipid environment by impacting phospholipid metabolism and disrupting lipid bilayers, which can inhibit TMEM117. Lastly, Ibuprofen affects the production of prostaglandins and other lipid signaling molecules, which could be crucial for TMEM117's functional role in cell signaling.