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Ribosomal protein S6 kinase II (RSK2) is a protein serine/threonine kinase that was originally detected by its ability to catalyze the multi-site phosphorylation of the 40S ribosomal protein S6 in vitro. One of the important substrates of RSK may be the Glycogenbinding subunit of Protein phosphatase-1, which when phosphorylated by RSK, appears to activate Protein phosphatase 1. This results in increased dephosphorylation and activation of Glycogen synthase to enhance Glycogen synthesis.