Year: 2012
Type: article
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.
Source: FEBS Open Bio
Institution: Kennesaw State University
Language: English
Subfield: Physiology
Field: Medicine
Domain: Health Sciences
Open Access status: gold
Estimated APC paid: $2,210
Awards: Purification of a Modified Flagellar Export Apparatus, RUI: Investigating novel mechanisms of MAPKAP Kinase 2 (MK2) regulation, Isoform specific effects of the autoinhibitory element and the C-terminus of nitr, G706898203, RUI: Domain Shuttle Mechanisms for Catalysis and Control in Nitric Oxide Synthases
OpenAlex ID: W2054850965