HDAC6 Protein, Human (His)

The HDAC6 protein assumes a multifaceted role, primarily responsible for the deacetylation of lysine residues on the N-terminal portion of core histones (H2A, H2B, H3, and H4), contributing to the epigenetic repression that plays crucial roles in transcriptional regulation, cell cycle progression, and developmental events. Operating within large multiprotein complexes, histone deacetylases, including HDAC6, orchestrate these processes. Beyond histones, HDAC6 extends its deacetylation activity to diverse proteins, such as tubulin, essential for microtubule-dependent cell motility, and alpha-tubulin, pivotal for cilia disassembly. Additionally, HDAC6 facilitates actin polymerization and autophagosome-lysosome fusion by deacetylating CTTN, promoting autophagy completion. Its involvement in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer and promotion of odontoblast differentiation showcase its diverse functions. Furthermore, HDAC6 plays a key role in the degradation of misfolded proteins, acting as an adapter to recognize polyubiquitinated misfolded proteins and targeting them to the aggresome for clearance via autophagy when the chaperone refolding system and the ubiquitin-proteasome are insufficient.