HDAC10 Inhibitors

HDAC10, a member of the histone deacetylase (HDAC) family, plays a significant role in regulating cellular processes through its enzymatic activity. This protein primarily functions as a histone deacetylase, catalyzing the removal of acetyl groups from lysine residues on histone proteins, thereby modulating chromatin structure and gene expression. However, HDAC10's involvement extends beyond histone deacetylation, as it also interacts with non-histone proteins, implicating its role in diverse cellular pathways such as cell cycle progression, DNA repair, and cellular differentiation. Through its regulatory actions on chromatin and protein substrates, HDAC10 exerts influence over various physiological processes crucial for cell viability and function. The inhibition of HDAC10 represents a pivotal strategy for elucidating its biological functions. HDAC inhibitors, both pan-HDAC inhibitors and isoform-selective inhibitors, have been developed to modulate HDAC activity. Mechanistically, HDAC inhibitors bind to the catalytic site of HDAC enzymes, thereby obstructing substrate access and impeding deacetylase activity. Consequently, inhibition of HDAC10 activity leads to alterations in histone acetylation patterns and perturbation of downstream signaling pathways associated with gene expression regulation. Additionally, HDAC inhibitors may induce changes in protein-protein interactions and protein stability, further influencing cellular processes regulated by HDAC10. Understanding the mechanisms underlying HDAC10 inhibition provides valuable insights into the physiological roles of this protein and offers opportunities for the development of novel interventions targeting HDAC-mediated pathways.