Molecular and Cellular Biology · 1996 · 64 citations · 42 references
Life SciencesBiochemistryMolecular BiologyCell SignalingGene ExpressionOncogenesEnzyme FunctionMacromolecular AssemblyProtein Complex AnalysisProtein Complex AssemblyProto-oncogene ActivationSignal Transduction ComplexesFootprintingMitogenic Signal TransductionPhosphorylation-dependent ActivationPhosphorylation-dependent RegulationQuaternary Structure FormationTernary Complex FormationTranscription Factor ComplexesTranscription Factor Dimerization
The rapid and transient induction of the human proto-oncogene c-fos in response to a variety of stimuli depends on the serum responses element (SRE). In vivo footprinting experiments show that this promoter element is bound by a multicomponent complex including the serum response factor (SRF) and a ternary complex factor such as Elk-1. SRF is thought to recruit a ternary complex factor monomer into an asymmetric complex. In this report, we describe a quaternary complex over the SRE which, in addition to an SRF dimer, contains two Elk-1 molecules. Its formation at the SRE is strictly dependent on phosphorylation of S-383 in the Elk-1 regulatory domain and appears to involve a weak intermolecular association between the two Elk-1 molecules. The influence of mutations in Elk-1 on quaternary complex formation in vitro correlates with their effect on the induction of c-fos reporter expression in response to mitogenic stimuli in vivo.
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Transformation of Mammalian Cells by Constitutively Active MAP Kinase Kinase
Sam J. Mansour, Wayne T. Matten, April S. Hermann et al. · Science · 1994 · 1.4K citations