FEBS open bio 2012,
PMID: 23650581
Chrestensen, Carol A; McMurry, Jonathan L; Salerno, John C
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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Text Mining Data
p38-eNOS ⊣ calmodulin: "
p38-eNOS binding was
inhibited by
calmodulin
"
p38-eNOS ⊣ calmodulin: "
p38-eNOS binding was inhibited by calmodulin
"
NOS ⊣ MAPK: "
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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