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- W2162474938 abstract "The extent and duration of MAPK (mitogen-activated protein kinase) signalling govern a diversity of normal and aberrant cellular outcomes. Genetic and pharmacological disruption of the MAPK-activated kinase RSK (ribosomal S6 kinase) leads to elevated MAPK activity indicative of a RSK-dependent negative feedback loop. Using biochemical, pharmacological and quantitative MS approaches we show that RSK phosphorylates the Ras activator SOS1 (Son of Sevenless homologue 1) in cultured cells on two C-terminal residues, Ser1134 and Ser1161. Furthermore, we find that RSK-dependent SOS1 phosphorylation creates 14-3-3-binding sites. We show that mutating Ser1134 and Ser1161 disrupts 14-3-3 binding and modestly increases and extends MAPK activation. Together these data suggest that one mechanism whereby RSK negatively regulates MAPK activation is via site-specific SOS1 phosphorylation." @default.
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- W2162474938 date "2012-09-12" @default.
- W2162474938 modified "2023-10-12" @default.
- W2162474938 title "RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively regulating MAPK activation" @default.
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- W2162474938 doi "https://doi.org/10.1042/bj20120938" @default.
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