Date published: 2025-9-13

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WDR27 Activators

Chemical activators of WDR27 can initiate various cellular signaling pathways, leading to its activation through phosphorylation. Forskolin, by raising intracellular cAMP levels, indirectly stimulates protein kinase A (PKA), which may then phosphorylate WDR27, altering its activity state. Similarly, dibutyryl-cAMP, a cAMP analog, diffuses into cells and mimics Forskolin's effects by also activating PKA, potentially resulting in the phosphorylation of WDR27. Phorbol 12-myristate 13-acetate (PMA) functions through a different mechanism, activating protein kinase C (PKC), which phosphorylates serine and threonine residues on a plethora of target proteins, possibly including WDR27. This post-translational modification can modulate WDR27's function within the cell. On another front, ionomycin increases intracellular calcium concentrations, which may activate calcium/calmodulin-dependent protein kinases (CaMKs). These kinases can phosphorylate various proteins within calcium-signaling pathways, potentially impacting WDR27's activation state.

Further, Calyculin A and Okadaic acid, both inhibitors of protein phosphatases PP1 and PP2A, prevent the dephosphorylation of proteins, which could lead to sustained phosphorylation and consequent activation of WDR27 if it is normally regulated by these phosphatases. Epigallocatechin gallate (EGCG) can activate AMP-activated protein kinase (AMPK), which may phosphorylate WDR27 directly or indirectly by targeting associated regulatory proteins. Similarly, Spermine NONOate releases nitric oxide that can increase cGMP levels, activating protein kinase G (PKG) that may phosphorylate and activate WDR27. Anisomycin, a stress-activated kinase activator, potentially involves WDR27 in the cellular response to stress by leading to its phosphorylation through activated Jun N-terminal kinase (JNK) pathways. Zaprinast inhibits phosphodiesterase 5, thereby increasing cGMP levels, which in turn may enhance PKG activity and lead to the phosphorylation of WDR27. Lastly, A23187 (Calcimycin), a calcium ionophore, raises cytosolic calcium levels, potentially leading to the activation of WDR27 through calcium-dependent protein kinases.

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