Chemical activators of ZNF773 can engage in various cellular mechanisms to facilitate its functional activation. Zinc Chloride provides essential zinc ions that are crucial for the structural integrity of zinc finger domains within ZNF773, ensuring proper folding and function. Forskolin acts upstream to elevate cAMP levels, subsequently activating protein kinase A (PKA). Activated PKA can target transcription factors like ZNF773, phosphorylating it to promote activation. Similarly, Dibutyryl-cAMP, a stable cAMP analog, functions within the same pathway, directly activating PKA which in turn is capable of phosphorylating and activating ZNF773.
Phorbol 12-myristate 13-acetate (PMA) is another agent that can activate ZNF773 through its action on protein kinase C (PKC). If ZNF773 contains PKC consensus sites, PMA-induced PKC activation can lead to its phosphorylation and activation. Ionomycin and A23187, both ionophores, raise intracellular calcium levels, which may activate calcium-dependent kinases that have the potential to phosphorylate and activate ZNF773. Thapsigargin serves a similar function by raising cytosolic calcium levels due to inhibition of the SERCA pump, potentially leading to the activation of kinases that can phosphorylate ZNF773. Anisomycin operates through the activation of the MAPK/ERK pathway, which is known to phosphorylate transcription factors, providing another route for the activation of ZNF773. Calyculin A and Okadaic Acid both prevent the dephosphorylation of proteins by inhibiting protein phosphatases 1 and 2A, which could lead to the sustained phosphorylation and consequent activation of ZNF773. Lastly, LY294002 inhibits PI3K, which might trigger the activation of alternative signaling pathways that can lead to the phosphorylation and activation of ZNF773, and Bisindolylmaleimide I, a PKC inhibitor, might similarly induce compensatory activation of pathways that converge on the phosphorylation and activation of ZNF773.
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