RNPC3 Inhibitors

Chemical inhibitors of RNPC3 disrupt its function by targeting the spliceosome, a crucial complex responsible for the splicing of pre-mRNA in cells. Pladienolide B and its derivative, Pladienolide D, bind to the SF3b complex within the spliceosome, where RNPC3 is a component. This binding inhibits the ability of RNPC3 to contribute to the splicing process. Similarly, E7107 acts on the same complex, leading to defective mRNA splicing and the inhibition of RNPC3 function within the spliceosome. Meayamycin B, another compound in this category, also impedes the functioning of the SF3b complex, resulting in the hampering of RNPC3 activity.

Additionally, Herboxidiene, also known as GEX1A, targets the spliceosome and consequently affects RNPC3's role in the splicing cycle by binding to a site near the SF3b complex. Isoginkgetin, a biflavonoid, interferes with the assembly of the spliceosome itself, which in turn impacts RNPC3's function. Madrasin and Spliceostatin A, both spliceosome inhibitors, bind to the SF3b complex, which directly affects RNPC3's role in mRNA splicing. Tetrocarcin A operates through a similar mechanism, disrupting RNPC3's involvement in the splicing process. FD-895, like the other chemical inhibitors mentioned, targets the spliceosome and binds to the SF3b complex, inhibiting splicing and thus RNPC3's function. Lastly, SSA, or spliceostatin A, binds to the same complex within the spliceosome, directly inhibiting the splicing activity of RNPC3. Each of these chemicals, by inhibiting the spliceosome, effectively hinders the splicing activity of RNPC3, showcasing a variety of molecular mechanisms that can lead to the inhibition of this protein's function.