Title

MAP Kinases Bind Endothelial Nitric Oxide Synthase

Department

Chemistry and Biochemistry

Document Type

Article

Publication Date

2-1-2012

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 (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.

Journal

FEBS Open Bio

Journal ISSN

2211-5463

Volume

2

Issue

1

First Page

51

Last Page

55

Digital Object Identifier (DOI)

10.1016%2Fj.fob.2012.02.002