SART-3 Activators

Chemical activators of SART-3 engage with the protein in various ways to enhance its activity related to RNA splicing. Resveratrol is known to activate sirtuin pathways such as SIRT1, which interacts with SART-3 to augment its deacetylase activity, thereby promoting its role in cellular stress responses. Similarly, spermidine can lead to the induction of autophagy, and through the inhibition of the acetyltransferase EP300, it can contribute to the functional enhancement of SART-3 by ensuring the recycling of spliceosomal components. Trichostatin A, as a histone deacetylase inhibitor, facilitates a relaxed chromatin state that provides splicing factors, including SART-3, with improved access to DNA for processing mRNA.

Furthermore, 5-Azacytidine's inhibition of DNA methyltransferases results in DNA hypomethylation, which may lead to the upregulation of genes that are involved in spliceosome assembly, thus fostering SART-3's role in RNA splicing. An analogous effect is seen with sodium butyrate, another histone deacetylase inhibitor, which increases chromatin accessibility and may enhance the activity of SART-3. In the context of protein degradation, MG132, a proteasome inhibitor, and disulfiram, which also inhibits the proteasome, can elevate the levels of snRNP components available for SART-3 action. Moreover, Leptomycin B, which inhibits protein export from the nucleus, increases the concentration of nuclear splicing factors and snRNPs, thereby augmenting SART-3's function. SAHA, similar to other histone deacetylase inhibitors, increases chromatin accessibility, which can lead to enhanced SART-3 activity. Chloroquine's inhibition of autophagy can indirectly increase the activity of SART-3 by causing an accumulation of cellular components like snRNPs. Lastly, beta-lapachone activates NQO1, which may influence SART-3's activity by altering the redox-sensitive cellular processes it is involved in.