CCDC91 Activators

Chemical activators of CCDC91 function by modulating the cellular levels of cyclic AMP (cAMP), a key secondary messenger in signal transduction pathways. Forskolin acts directly on adenylate cyclase, the enzyme responsible for converting ATP to cAMP, resulting in an increase in cAMP levels within the cell. This boost in cAMP activates protein kinase A (PKA), which then phosphorylates CCDC91, thereby influencing its activity. Similarly, IBMX increases cAMP concentrations by inhibiting phosphodiesterases, enzymes that degrade cAMP. This leads to sustained activation of PKA, which in turn can phosphorylate CCDC91. Epinephrine and isoproterenol, through their interactions with adrenergic receptors, also stimulate adenylate cyclase, causing a rise in cAMP and subsequent PKA-mediated phosphorylation of CCDC91. PGE2 and histamine operate through their respective G-protein coupled receptors to elevate cAMP and activate PKA, which then targets CCDC91 for phosphorylation.

The action of dopamine, like that of epinephrine and histamine, involves stimulation of G-protein coupled receptors leading to increased adenylate cyclase activity and elevated cAMP levels, which facilitate PKA activation and subsequent phosphorylation of CCDC91. Cholera toxin permanently activates the Gs alpha subunit, causing relentless stimulation of adenylate cyclase and a consequent chronic increase in cAMP, which results in PKA engaging in the continuous phosphorylation of CCDC91. Rolipram, by selectively inhibiting phosphodiesterase 4, and anagrelide, through inhibition of phosphodiesterase III, both prevent the breakdown of cAMP, thereby enhancing PKA activity and promoting the phosphorylation of CCDC91. Beta-adrenergic agonists like terbutaline and salbutamol bind to their respective receptors and stimulate adenylate cyclase, increasing cAMP levels. This elevation in cAMP enables PKA to phosphorylate CCDC91, influencing its activity within the cell.