Forskolin binds directly to adenylate cyclase, catalyzing an increase in the levels of cAMP, a pivotal second messenger within the cell. This surge in cAMP triggers the activation of PKA, an enzyme that can phosphorylate a range of substrates, including proteins similar to FLJ46082. In this manner, Forskolin's effect is established through a classic signaling cascade that culminates in protein activation.
Conversely, inhibitors like H-89, despite their primary role in suppressing PKA activity, can instigate a cellular feedback loop that indirectly activates alternative pathways leading to the activation of proteins paralleling FLJ46082. Genistein, by impeding protein tyrosine kinases, precipitates a shift in phosphorylation balance, which can cascade down to affect the activation status of a variety of proteins, potentially including FLJ46082. Chemical agents such as LY294002 and PD98059, known for their inhibitory action on the PI3K/Akt and MEK/ERK pathways respectively, exert their effects by disrupting the normal phosphorylation of proteins within these pathways. This disruption can lead to an altered functional state of proteins engaged in these signaling cascades, thereby indirectly influencing the activation of FLJ46082.
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