Rsk Mouse, Unlabeled, Clone: 78, BD

Description

• The p90[rsk] (Rsk) and p70[s6k] kinases were first identified based on their ability to phosphorylate the 40S ribosomal protein S6 in vitro
• Both of these enzymes are differentially regulated by serine/threonine phosphorylation in response to mitogenic stimulation
• ERK1 and ERK2 have been shown to regulate Rsk activity
• Once activated by this phosphorylation, a significant amount of Rsk can be found in the nucleus, suggesting that it has a role in nuclear signaling events
• The regulation of nuclear Rsk and ERK activities by growth factors is coordinated with the induction of several early response genes
• Rsk has also been shown to be activated by ionizing radiation, presumably through an activated MAP kinase
• Studies in Xenopus oocytes and mouse NIH/3T3 cells indicate that inactive Rsk and ERK2 exist in a complex of approximately 110kDa
• Upon phosphorylation of Rsk and ERK2, the heterodimer dissociates and at least a portion of these activated kinases translocate to the nucleus.