CCDC90B Activators

CCDC90B can modulate its activity through various cellular signaling pathways that converge on the mitochondria. Sildenafil and Zaprinast, by inhibiting phosphodiesterase 5, lead to elevated cGMP levels within the cell. Elevated cGMP can activate protein kinases that have the capacity to phosphorylate mitochondrial proteins, thereby enhancing the activity of CCDC90B. Similarly, Isoproterenol, a beta-adrenergic agonist, increases intracellular cAMP, which subsequently activates protein kinase A (PKA). PKA can then target proteins within the mitochondria, including CCDC90B, to modulate their activity. This is akin to the action of Forskolin, which directly activates adenylyl cyclase, resulting in a rise in cAMP levels and the activation of PKA, with downstream effects on mitochondrial proteins like CCDC90B. Dibutyryl-cAMP, serving as a cAMP analog, bypasses cell surface receptors and directly provides an elevation in cAMP within the cell, leading to PKA activation and subsequent modulation of CCDC90B activity.

Glucagon, through its receptor-mediated activation of adenylyl cyclase, similarly raises cAMP levels, thereby activating PKA which can phosphorylate mitochondrial proteins including CCDC90B. Rolipram, by selectively inhibiting phosphodiesterase 4, also causes an accumulation of cAMP, which then activates PKA and can enhance the activity of CCDC90B. The activation of AMP-activated protein kinase (AMPK) by AICAR initiates a cellular cascade that can lead to improved mitochondrial function and possibly an increase in the activity of CCDC90B. Nicotinamide riboside, by increasing NAD+ levels, provides substrates for sirtuins that deacetylate and activate mitochondrial proteins, which may include CCDC90B. Resveratrol acts similarly by activating sirtuins, which can affect CCDC90B activity. The PGC-1α activator (CAY10610) promotes the expression of mitochondrial proteins, which can enhance mitochondrial function and potentially the activity of CCDC90B within the organelle. Lastly, BAY 60-6583, by acting as an adenosine A2B receptor agonist, elevates cAMP, which activates PKA, potentially leading to phosphorylation and modulation of CCDC90B activity within the mitochondria.