U2AF35 Activators

U2AF35 activators are a group of chemicals that modulate the activity of U2AF35, a protein that plays a critical role in the splicing of pre-mRNA in eukaryotic cells. U2AF35, also known as U2AF1, is part of the U2 auxiliary factor complex that recognizes and binds to the polypyrimidine tract adjacent to the 3' splice site of introns. Its role is essential for the proper assembly of the spliceosome, the complex molecular machine that removes introns from pre-mRNA transcripts.

Direct activators of U2AF35 enhance its RNA-binding affinity or its interaction with other spliceosomal components, thereby facilitating the splicing process. This can occur through a conformational change in the U2AF35 protein that increases its ability to recruit U2AF65, another spliceosome component, to the pre-mRNA substrate. Alternatively, a direct activator might stabilize the U2AF35 protein or protect it from proteolytic degradation, thus ensuring a more robust presence in the splicing machinery. Indirect activators may work by upregulating the expression of the U2AF35 gene, thereby increasing the protein's abundance in the cell. They could also modulate post-translational modifications of U2AF35, such as phosphorylation, which can affect its activity and interactions. Furthermore, indirect activators could influence the splicing machinery by affecting the availability or function of cofactors and other proteins that interact with U2AF35 to regulate splice site selection and splicing efficiency.