LOC729160 Activators

Forskolin directly targets adenylyl cyclase, resulting in elevated cAMP levels that activate PKA. PKA then phosphorylates various proteins, potentially altering their function. Similarly, phorbol esters such as PMA activate PKC, which in turn can phosphorylate a multitude of proteins across different pathways, affecting their activity. Ionomycin, by increasing intracellular calcium, can activate numerous calcium-dependent proteins, while sodium orthovanadate maintains proteins in a phosphorylated state by inhibiting tyrosine phosphatases, thus affecting proteins that are regulated by phosphorylation on tyrosine residues.

Isoproterenol acts on beta-adrenergic receptors, leading to an increase in intracellular cAMP and subsequent activation of PKA. Retinoic acid binds to and activates nuclear receptors that modulate gene expression, thereby influencing the activity of various proteins. cAMP analogs, such as 8-Bromo-cAMP and Dibutyryl-cAMP, activate PKA, leading to changes in protein activity through phosphorylation. EGCG has the ability to modulate various signaling pathways, potentially altering protein activity through modifications in phosphorylation patterns. Inhibitors like LY294002 and SB203580, by targeting key kinases such as PI3K and p38 MAP kinase respectively, can lead to the modulation of protein activity within their respective pathways, demonstrating that even inhibitors can serve as indirect activators through the complex interplay of cellular signaling networks.