PPP2R3C activators function by manipulating the phosphorylation state within the cell, thereby influencing the activity of the protein. For example, certain small molecules can increase intracellular cyclic AMP levels, which in turn activate protein kinase A. The active kinase A then phosphorylates inhibitory proteins that regulate PPP2R3C, which reduces their ability to inhibit this phosphatase, resulting in its activation. Alternatively, some activators work by preventing the degradation of cyclic nucleotides, leading to sustained activation of kinase pathways that ultimately enhance the activity of PPP2R3C. Phosphoprotein phosphatase inhibitors, such as those that target PP1 and PP2A, lead to an overall increase in the phosphorylation levels within the cell. This buildup of phosphorylated substrates can trigger a feedback mechanism, potentially involving PPP2R3C, to restore phosphorylation balance. Moreover, certain inhibitors directly enhance the phosphorylation state of proteins that are known to interact with PPP2R3C, thereby facilitating its activation.
Other mechanisms by which PPP2R3C activators exert their influence include the modulation of protein kinase C, which phosphorylates and activates PPP2R3C or its upstream regulators. Some activators mimic natural ligands, binding to receptors and initiating signaling cascades that result in the activation of PPP2R3C. For instance, lipid signaling pathways can be influenced by activators that change the levels of diacylglycerol (DAG) or phosphatidylinositol bisphosphate (PIP2), both of which are known to activate protein kinase C (PKC).
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