TAF II p70 Inhibitors

Chemical inhibitors of TAF II p70 target the protein's role in the transcription initiation complex through various modes of action, primarily by disrupting its interaction with chromatin. Trichostatin A, mocetinostat, entinostat, vorinostat, belinostat, panobinostat, romidepsin, quisinostat, and givinostat all function as histone deacetylase (HDAC) inhibitors. These inhibitors lead to an increase in histone acetylation levels, which in turn can alter the chromatin structure. By changing the acetylation status of histones, these chemical inhibitors can interfere with the normal interactions of TAF II p70 with chromatin, thereby inhibiting its function within the transcription initiation complex. The alteration of chromatin structure is a key mechanism by which these compounds exert their effects on TAF II p70, as the protein's ability to engage with chromatin is essential for its role in initiating transcription.

Flavopiridol operates through a different mechanism, acting as a cyclin-dependent kinase inhibitor. By inhibiting these kinases, flavopiridol can reduce the phosphorylation of proteins that are associated with TAF II p70, which may be crucial for TAF II p70's functional activity in the transcription initiation process. Selisistat, on the other hand, targets sirtuin enzymes, a class of HDACs, which also play a role in deacetylating histones. Through the inhibition of sirtuin activity, selisistat can lead to changes in the acetylation pattern of chromatin, thus affecting TAF II p70's interaction with chromatin. CUDC-907 is unique in that it not only inhibits HDACs but also targets phosphoinositide 3-kinase (PI3K). Although the PI3K inhibition is not directly related to the modulation of TAF II p70, the compound's HDAC inhibitory activity can affect the protein's interaction with chromatin, which is crucial for its role in the transcription initiation complex.