Proceedings of the National Academy of Sciences · 1995 · 152 citations · 33 references
Life SciencesBiochemistryMolecular BiologyCell SignalingGene ExpressionSignal TransductionMyc Family OncogenesOncogene ActivationProtein Kinase CascadesSignal Transduction ComplexesExtracellular Signal-regulated Kinase PathwayExtracellular Signal-regulated Kinase SignalingHelix-loop-helix MotifKinase Substrate SpecificityMitogen-activated Protein Kinase KinaseMitogen-activated Protein Kinase SignalingMyc OncogenesMyc Proto-oncogene
We describe Mxi2, a human protein that interacts with Max protein, the heterodimeric partner of the Myc oncoprotein. Mxi2 encodes a 297-residue protein whose sequence indicates that it is related to extracellular signal-regulated kinases (ERK protein kinases). Mxi2 in yeast interacts with Max and with the C terminus of c-Myc. Mxi2 phosphorylates Max both in vitro and in vivo. The Mxi2 putative substrate recognition region has sequence similarity to the helix-loop-helix region in Max and c-Myc, suggesting that substrate recognition might be mediated via this motif. Phosphorylation by Mxi2 may affect the ability of Max to oligomerize with itself and its partners, bind DNA, or regulate gene expression.
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