GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins
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2021, Cell Chemical BiologyCitation Excerpt :Membrane attachment can also be regulated by ubiquitination (Baietti et al., 2016; Steklov et al., 2018; Thurman et al., 2020), phosphorylation of the C terminus as well as other post-translational modifications, such as acetylation, and calmodulin (Jang et al., 2017, 2019; Nussinov et al., 2017b). As members of the small GTPase family, Ras proteins function as molecular switches between their two states (Bourne et al., 1991; Cherfils and Zeghouf, 2013; Downward, 1990; Geyer and Wittinghofer, 1997; Grand and Owen, 1991; Lamontanara et al., 2014; Lowy et al., 1991; Sprang, 1997; Takai et al., 2001; Vetter and Wittinghofer, 2001; Wittinghofer and Pai, 1991; Wittinghofer and Vetter, 2011). Inactivation is mediated by GTPase-activating proteins (GAPs) that hydrolyze the GTP to GDP (Wittinghofer et al., 1997).
Development of Noonan syndrome by deregulation of allosteric SOS autoactivation
2020, Journal of Biological ChemistryA KRAS GTPase K104Q mutant retains downstream signaling by offsetting defects in regulation
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