Rsk Inhibitors

Ribosomal S6 kinase (RSK) is a family of serine/threonine protein kinases that are involved in regulating multiple cellular processes including cell growth, proliferation, differentiation, and survival. RSK is a downstream target of the mitogen-activated protein kinase (MAPK) pathway and is activated by phosphorylation by extracellular signal-regulated kinases 1 and 2 (ERK1/2), p38 MAPK, and other protein kinases. The RSK family consists of four isoforms (RSK1-4) which are expressed in different tissues and have distinct functions. RSK1 and RSK2 are widely expressed and play roles in cell proliferation and survival, while RSK3 and RSK4 are primarily expressed in the brain and have been implicated in neuronal development and synaptic plasticity The Rsk Inhibitors class comprises a diverse array of chemicals designed to selectively target and inhibit the activity of Ribosomal S6 Kinase (Rsk), a family of serine/threonine kinases involved in crucial cellular processes. BI-D1870, a prominent member of this class, is a potent inhibitor that acts by blocking the kinase activity of Rsk, specifically disrupting the phosphorylation of its activation loop. This disruption of Rsk's activation loop phosphorylation leads to the inhibition of downstream signaling pathways regulated by Rsk, providing researchers with a powerful tool to investigate the functional consequences of Rsk inhibition in various cellular contexts. LJI308 is another notable inhibitor that competes with ATP for binding to Rsk's kinase domain. By binding to the ATP-binding site, LJI308 hampers Rsk's activation and subsequent phosphorylation of downstream substrates. This inhibition disrupts Rsk-mediated signaling pathways involved in cellular proliferation and survival, positioning LJI308 as a valuable compound for elucidating the role of Rsk in diverse cellular processes. The class also includes SL0101, a selective inhibitor that interferes with Rsk's activation loop phosphorylation. This disruption of Rsk's phosphorylation status suppresses its kinase activity, unraveling the intricate regulatory mechanisms of Rsk-mediated signaling pathways.