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MAP Kinanses Bind Endothelial Nitric Oxide Synthase
FEBS Open Bio (2012)
  • Carol A. Chrestensen, Kennesaw State University
  • Jonathan McMurry
  • John C. Salerno
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 (kon ∼ .15 × 106 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.
  • Nitric oxide synthase,
  • MAP kinase,
  • ERK; p38,
  • Optical biosensing
Publication Date
Citation Information
Carol A. Chrestensen, Jonathan McMurry and John C. Salerno. "MAP Kinanses Bind Endothelial Nitric Oxide Synthase" FEBS Open Bio Vol. 2 (2012) p. 51 - 55
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