Key result
MAP kinases p38 and ERK bind eNOS with ~100 nM affinity, suggesting direct NOS regulation.
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The direct binding of MAP kinases to eNOS suggests a novel regulatory mechanism for nitric oxide synthesis, with potential implications for angiogenesis and vascular tone.
Endothelial nitric oxide synthase (eNOS) contains a motif similar to recognition sequences in known MAPK binding partners. In optical biosensing experiments, eNOS bound p38 and ERK with ∼100 nM affinity and complex kinetics. Binding is diffusion-limited (k on ∼ .15 × 10(6) M(-1) s(-1)). Neuronal NOS also bound p38 but exhibited much slower and weaker binding. p38-eNOS binding was inhibited by calmodulin. Evidence for a ternary complex was found when eNOS bound p38 was exposed to CaM, increasing the apparent dissociation rate. These observations strongly suggest a direct role for MAPK in regulation of NOS with implications for signaling pathways including angiogenesis and control of vascular tone.
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Chrestensen et al. (2012) studied this question. MAP kinases (p38 and ERK) was evaluated on Binding affinity and kinetics. Endothelial nitric oxide synthase bound p38 and ERK with ~100 nM affinity and complex kinetics, suggesting a direct role for MAPK in the regulation of NOS.
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