Date published: 2025-9-12

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MTERFD3 Activators

Chemical activators of MTERFD3 can engage various cellular signaling pathways to enhance the functional activity of this protein. Forskolin, by activating adenylate cyclase, boosts intracellular cAMP levels, leading to the activation of protein kinase A (PKA). PKA, in turn, can phosphorylate MTERFD3, thereby increasing its activity. Similarly, 8-Bromo-cAMP, a cAMP analog, directly activates PKA, again leading to potential phosphorylation and activation of MTERFD3. These pathways underscore the role of phosphorylation as a key regulatory mechanism for MTERFD3 activity. Ionomycin and A23187 both act as calcium ionophores, which escalate intracellular calcium concentrations. Elevated calcium levels activate calcium-dependent protein kinases that can phosphorylate MTERFD3, thus promoting its activation. Thapsigargin also elevates intracellular calcium by inhibiting the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA), leading to a similar activation cascade for MTERFD3 through calcium-mediated kinase activation.

The use of phorbol esters like Phorbol 12-myristate 13-acetate (PMA) and TPA directly activates protein kinase C (PKC), which may phosphorylate and activate MTERFD3. Chelerythrine, though it inhibits PKC, can result in the compensatory activation of alternative kinases that contribute to MTERFD3 phosphorylation and activation. Anisomycin activates stress-activated protein kinases that can also contribute to MTERFD3 phosphorylation and activation. Compounds like Calyculin A and Okadaic Acid prevent the dephosphorylation of proteins by inhibiting specific phosphatases, thus maintaining MTERFD3 in a phosphorylated and active state. Additionally, Isoproterenol, as a beta-adrenergic agonist, increases cAMP, activating PKA, which could also phosphorylate MTERFD3. Collectively, these chemicals employ various strategies to ensure the phosphorylation state of MTERFD3, which is critical for its activation. Each pathway converges on the phosphorylation of MTERFD3, establishing it as a pivotal point of control for the activation of this protein.

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