p-Rsk-1 Anticuerpo(Ser 363): sc-135634

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The family of ribosomal S6 kinases (Rsks), designated Rsk-1, Rsk-2 and Rsk-3, are important signaling intermediates that mediate responses to a broad range of ligand-activated receptor tyrosine kinases. It has been established that Rsk-3 is not activated by MAP kinase in vitro, unlike Rsk-1 and Rsk-2. A unique feature common to the three members of the Rsk family is that each possesses two non-identical complete kinase catalytic domains. The Rsk family amino-terminal kinase domain is phosphorylated on Ser 227 by 3-phosphoinositide-dependent protein kinase-1 (PDK1), which increases the kinase activity of Rsk. In the carboxy-terminal kinase domain, Rsk-1 and Rsk-2 are autophosphorylated on Ser 380 and Ser 386, respectively, which mediates the docking of PDK1 to Rsk in order to promote phosphorylation of substrates, such as histone H3. Human, rat and mouse Rsk-1 are activated by phosphorylation on threonine and serine residues, such as Ser 363.