Gm70 Activators

PPP1R36 activators comprise a diverse group of chemical compounds that modulate the activity of protein phosphatase 1, regulatory subunit 36 (PPP1R36), a component of the protein phosphatase 1 (PP1) complex. This complex plays a crucial role in cellular processes by reversing the phosphorylation of serine and threonine residues on proteins, which is a post-translational modification that can alter the function, localization, and interaction of proteins within the cell. The activators of PPP1R36 do not directly stimulate the regulatory subunit but rather influence the phosphorylation state of proteins that PPP1R36 may bind to or regulate. These compounds achieve this modulation through a variety of mechanisms, each interacting with different molecular pathways to indirectly affect the activity of PPP1R36. Some activators, such as Okadaic Acid and Calyculin A, are known to inhibit PP1, leading to an overall increase in the phosphorylated forms of proteins within the cell. This increase in phosphorylation can, in turn, augment the availability of substrates that PPP1R36 may act upon.

The significance of these activators lies in their ability to alter the dynamics of protein phosphorylation, which is a critical regulatory mechanism in cells. By affecting the enzyme's substrate availability or the interaction between PPP1R36 and its protein targets, these compounds can influence the functional state of PPP1R36. For example, agents that upregulate intracellular cAMP levels, such as Forskolin, indirectly promote PPP1R36 activity by activating protein kinase A (PKA), which can then phosphorylate proteins that are potential substrates for PPP1R36. Other activators work by different mechanisms: Phorbol 12-myristate 13-acetate (PMA) functions by activating protein kinase C (PKC), which phosphorylates a broad range of proteins, potentially altering the substrate recognition by PPP1R36. Ionomycin, a calcium ionophore, can elevate intracellular calcium concentrations, thereby activating calcium-dependent calmodulin kinases (CaMKs) which also phosphorylate numerous cellular proteins.