HAPSTR2 Activators

Activators of HAPSTR2 employ a variety of mechanisms to enhance its functional activity, primarily through the modulation of phosphorylation states and second messenger systems. For instance, the stimulation of adenylyl cyclase activity by certain compounds leads to a rise in intracellular cAMP levels, which in turn activates protein kinase A (PKA). The activated PKA can then phosphorylate HAPSTR2, increasing its activity. Additionally, the inhibition of phosphodiesterases plays a crucial role in maintaining elevated levels of cAMP and cGMP, further sustaining the activation of HAPSTR2 through PKA and other cGMP-dependent protein kinases. Moreover, the activation of AMP-activated protein kinase (AMPK) in response to energy stress also triggers a cascade of phosphorylation events that can culminate in the enhanced activity of HAPSTR2.

Another set of activators works by modulating protein kinase C (PKC) and adenosine A2B receptors, which are known to influence intracellular signaling cascades that can lead to the phosphorylation and subsequent activation of HAPSTR2. Certain inhibitors of tyrosine kinases can also result in altered phosphorylation patterns that favor the activation of HAPSTR2. Beyond these, phosphatase inhibitors contribute to the activation of HAPSTR2 by preventing the dephosphorylation of proteins, thereby promoting a sustained phosphorylated state that supports the active conformation of HAPSTR2.