CHMP7 Inhibitors

Chemical inhibitors of CHMP7 can affect its function in various cellular processes including endosomal sorting, membrane remodeling, and nuclear envelope reformation. Alloxazine interferes with the ESCRT-III complex assembly, of which CHMP7 is a crucial component, by hindering the polymerization and membrane remodeling activities that are essential for the complex's function. Aurintricarboxylic Acid disrupts CHMP7's interaction with nucleic acids, which is necessary for its role in chromatin organization and nuclear envelope reformation. Bafilomycin A1's inhibition of vacuolar H+ ATPase can lead to dysregulation of endosomal acidification, thus affecting the endosomal sorting functions involving CHMP7. Ebselen, through its redox-modulating activities, can alter the assembly of the ESCRT-III complex, thereby impairing CHMP7's function in membrane remodeling. Dynasore's inhibition of GTPase activity affects dynamin-related proteins, which play a role in the membrane scission events that are supported by CHMP7.

Furthermore, Mitoxantrone, by intercalating into DNA, can impede the DNA-protein interactions necessary for CHMP7's function during mitotic exit. Myricetin inhibits phosphoinositide 3-kinases that participate in signaling pathways regulating membrane trafficking events in which CHMP7 is involved, thereby affecting its function. Neomycin, by binding to phospholipids, can disrupt membrane integrity and consequently impair CHMP7's role in endosomal sorting. Nocodazole disrupts microtubule dynamics, essential for CHMP7's proper localization and function in cellular division and membrane reformation. Okadaic Acid alters the phosphorylation state of proteins within the ESCRT pathway, influencing CHMP7's role in the complex. U18666A induces intracellular cholesterol accumulation, altering membrane properties and subsequently affecting CHMP7's recruitment and function in membrane remodeling processes. Lastly, zinc ions can bind to and alter the function of metalloproteins and enzymes, potentially disrupting the enzymatic activities required by CHMP7 to fulfill its role in endosomal sorting and membrane fusion.