Gemin7 Inhibitors

Chemical inhibitors of Gemin7 function by interfering with various stages of the splicing process and snRNP assembly, in which Gemin7 plays a crucial role. Amiloride, by disrupting cellular ion transport, can indirectly affect cellular processes including those linked to snRNP assembly, potentially inhibiting Gemin7. Pladienolide B, Madrasin, Meayamycin, E7107, Herboxidiene, Spliceostatin A, and Isoginkgetin all target components of the spliceosome. Pladienolide B, for instance, binds to the SF3b complex disrupting its function; since Gemin7 is part of the spliceosomal machinery, its function is indirectly inhibited when the SF3b complex is compromised. Similarly, Madrasin and E7107 inhibit the spliceosomal U2 snRNP, and Meayamycin, Sudemycin D6, and Spliceostatin A interact with the SF3b complex. By binding to these components, they disrupt the proper assembly and function of the spliceosome, thus inhibiting the role of Gemin7 in snRNP assembly. Further, Herboxidiene's action on the spliceosome can affect the formation and function of snRNPs and, consequently, inhibit Gemin7. Isoginkgetin, as a splicing inhibitor, disrupts the spliceosome assembly, which potentially hampers Gemin7's involvement in snRNP biogenesis. Plitidepsin interacts with eEF1A2, a factor necessary for protein synthesis, and by doing so, can indirectly inhibit Gemin7 by affecting snRNP assembly. Silvestrol, an eIF4A inhibitor, can also inhibit protein synthesis, affecting the production of proteins vital for Gemin7's function in snRNP assembly. Lastly, Toyocamycin, an adenosine analog, by inhibiting RNA processing, can disrupt snRNP assembly or function, which would inhibit the function of Gemin7 within the spliceosome, as Gemin7 is integral to the proper functioning of this cellular machinery.