DNAHC12 Activators

DNAH12, encoding the dynein axonemal heavy chain 12, plays a crucial role in microtubule-based movement. Predicted to be located in cilium, cytoplasm, and microtubule, it is part of the dynein complex. The activation of DNAH12 involves intricate molecular events influenced by various chemical activators. Lithium chloride, by stabilizing β-catenin and promoting its nuclear translocation, enhances DNAH12 transcription. Forskolin elevates cAMP levels, activating PKA, which phosphorylates CREB, facilitating DNAH12 activation. Sodium butyrate, through histone deacetylase inhibition, creates a permissive chromatin state for DNAH12 transcription. Retinoic acid, binding to retinoic acid receptors, directly activates DNAH12 by enhancing its transcription. Dibutyryl cyclic AMP mimics endogenous cAMP, activating PKA and promoting DNAH12 transcription. Trichostatin A inhibits histone deacetylases, altering chromatin structure for DNAH12 activation. Dimethyl sulfoxide modulates the NF-κB pathway, preventing its inhibitory effect on DNAH12. 5-Azacytidine promotes DNA demethylation, facilitating DNAH12 transcription. Valproic acid inhibits histone deacetylases, creating a permissive chromatin environment for DNAH12 activation.

2-Aminopurine directly activates DNAH12 by inhibiting PKR, relieving its inhibitory effect on DNAH12 translation. Sodium valproate, through histone deacetylase inhibition, promotes DNAH12 transcription. Epigallocatechin gallate indirectly activates DNAH12 by inhibiting MEK in the MAPK/ERK pathway, relieving SPRY4-mediated inhibition and promoting DNAH12 transcription. This comprehensive understanding of DNAH12 activation sheds light on avenues for modulation, providing insights into its role in microtubule-based movement within cells.