title: MAP kinases bind endothelial nitric oxide synthase.
abstract: 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.
authors: Department of Chemistry & Biochemistry, Kennesaw State University, Kennesaw, GA 30144-1203, USA.
authors: Carol A
authors: CA
authors: Chrestensen
authors: Jonathan L
authors: JL
authors: McMurry
authors: John C
authors: JC
authors: Salerno
keywords: AI, autoinhibitory element of nitric oxide synthase; ATF, activating transcription factor; Akt, v-akt murine thymoma viral oncogene homolog 1 (a.k.a, protein kinase B); BAEC, bovine aortic endothelial cells; CaM, calmodulin; ERK; ERK1/2, mitogen activated protein kinase 1 and 2; MAP kinase; MEF, myocyte enhancer factor; MK or MAPKAP kinase, mitogen activated protein kinase activated protein kinase; Nitric oxide synthase; Optical biosensing; PKA, protein kinase A; eNOS, endothelial nitric oxide synthase; nNOS, neuronal nitric oxide synthase; p38
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