Monoubiquitylation activates RAS isoforms through an unknown mechanism. Using NMR spectroscopy, computational modelling and biochemistry, Baker and colleagues found that KRAS monoubiquitylation does not affect GTP binding, GTP hydrolysis or the regulation of RAS–GDP exchange. Rather, monoubiquitylation of K147 substantially reduced the response of KRAS to GTPase-activating proteins, which results in prolonged activation of KRAS (as it remains GTP bound).
ORIGINAL RESEARCH PAPER
Baker, R. et al. Site-specific monoubiquitination activates Ras by impeding GTPase-activating protein function. Nature Struct. Mol. Biol. 25 Nov 2012 (doi:10.1038/nsmb.2430)
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Alderton, G. Modifying responses. Nat Rev Cancer 13, 7 (2013). https://doi.org/10.1038/nrc3444
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DOI: https://doi.org/10.1038/nrc3444
