U2AF1L3 Activators

U2AF1L3 function by modulating the cellular levels of cyclic AMP (cAMP), a second messenger with a key role in signal transduction. Forskolin is known to directly increase cAMP levels within cells by activating adenylate cyclase. The elevation of cAMP facilitates the activation of protein kinase A (PKA), which in turn is capable of phosphorylating and activating serine/arginine-rich (SR) proteins, including U2AF1L3. Similarly, Epigallocatechin gallate has the capacity to inhibit phosphodiesterases, leading to an increase in cAMP. This sequence of events also culminates in the phosphorylation of U2AF1L3 by PKA. Another compound, Dibutyryl-cAMP, a cAMP analog, permeates cellular membranes and directly activates PKA without the need for upstream cAMP generation, prompting a similar phosphorylation and activation of U2AF1L3.

Isoproterenol, a beta-adrenergic agonist, elevates intracellular cAMP levels, thus instigating a cascade that results in PKA-mediated phosphorylation of U2AF1L3. Rolipram and Anagrelide, by selectively inhibiting phosphodiesterase 4 and phosphodiesterase III, respectively, prevent the breakdown of cAMP, thereby sustaining PKA activation and subsequent U2AF1L3 phosphorylation. Prostaglandins E1 (PGE1) and E2 (PGE2) activate adenylate cyclase, which catalyzes the conversion of ATP to cAMP, again leading to PKA activation and phosphorylation of U2AF1L3. IBMX, a non-selective phosphodiesterase inhibitor, raises cAMP levels, resulting in PKA activation and U2AF1L3 phosphorylation. Lastly, Luteolin, Vinpocetine, and Zaprinast, all phosphodiesterase inhibitors, increase cAMP levels, which in turn activate PKA, and this activation leads to the phosphorylation of U2AF1L3. Through these mechanisms, these diverse chemicals can lead to the activation of U2AF1L3 via phosphorylation by PKA.