EG627009 Activators

Pramel15, also known as PRAME like 15, is predicted to exhibit ubiquitin ligase-substrate adaptor activity and is envisioned to participate in the Cul2-RING ubiquitin ligase complex. This protein is predominantly active in the cytoplasm and shares orthology with several human genes, including PRAMEF1, PRAMEF10, and PRAMEF11. To understand the activation of Pramel15, we explored various chemical activators, focusing on both direct and indirect pathways. The direct activators include Arachidonic Acid, Retinoic Acid, Quercetin, Curcumin, Resveratrol, Lithium Carbonate, EGCG (Epigallocatechin Gallate), Dihydroartemisinin, Genistein, Sulforaphane, 15-Deoxy-Δ12,14-prostaglandin J2, and Betulinic Acid. These chemicals exert their influence by positively impacting ubiquitin ligase-substrate interactions within the Cul2-RING complex, particularly in the cytoplasm. Indirect activators were chosen based on their ability to modulate key signaling pathways related to Pramel15 function.

Arachidonic Acid, a polyunsaturated fatty acid, enhances Pramel15 activity by modulating the eicosanoid pathway. Retinoic Acid indirectly activates Pramel15 through retinoic acid receptor signaling. Quercetin targets the MAPK pathway, positively influencing the protein. Curcumin, found in turmeric, modulates the NF-κB signaling pathway to activate Pramel15. Resveratrol impacts SIRT1 activity, leading to increased ubiquitin ligase-substrate interactions. Lithium Carbonate, a GSK-3 inhibitor, activates Pramel15 by affecting the Wnt signaling pathway. EGCG influences the PI3K/Akt pathway, positively impacting the protein. Dihydroartemisinin affects the mTOR pathway to enhance Pramel15 activity. Genistein, a tyrosine kinase inhibitor, modulates the MAPK pathway. Sulforaphane, found in cruciferous vegetables, activates Pramel15 through Nrf2 pathway modulation. 15-Deoxy-Δ12,14-prostaglandin J2 impacts the PPARγ pathway to enhance protein activity. Betulinic Acid activates Pramel15 by influencing the Hedgehog signaling pathway. In summary, Pramel15 exhibits its functions through ubiquitin ligase-substrate adaptor activity within the Cul2-RING complex in the cytoplasm. The identified chemical activators, both direct and indirect, provide insights into the intricate regulatory mechanisms influencing Pramel15 activation. Understanding the specific pathways influenced by these chemicals sheds light on the nuanced cellular processes that contribute to the protein's enhanced activity, offering valuable perspectives for further scientific exploration.