کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1981840 | 1539422 | 2012 | 5 صفحه PDF | دانلود رایگان |
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.
▸ MAP kinases bind to a pentabasic sequence in the eNOS autoinhibitory insertion. ▸ MAP kinases bind poorly or not at all to nNOS. ▸ MAP kinases interact weakly with CaM binding, increasing CaM release. ▸ The MAPK binding site is adjacent to the phosphorylation sites of other kinases.
Journal: FEBS Open Bio - Volume 2, 2012, Pages 51–55