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Updated: Aug 17, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor
Mónica Martínez-Moreno1, Alberto Alvarez-Barrientos, Fernando Roncal
1Departamento de Bioquímica y Biología Molecular, Facultad CC. Químicas, Universidad Complutense, 28040 Madrid, Spain.
Abstract:
We have performed the recombinant expression and purification of the reductase domain of endothelial nitric oxide synthase (eNOS) and used it as a bait in search for interacting proteins present in endothelial cells. Using mass spectrometry of the bound proteins run in a PAGE-SDS gel, we were able to identify the ryanodine receptor (RyR) as a novel eNOS-binding partner. This interaction was confirmed through immunoprecipitation of both RyR and eNOS from endothelial cells and cardiac myocytes. Immunofluorescence data indicated that a subpopulation of eNOS associates with RyR in perinuclear regions of the cell, where eNOS might be responsible for the known nitrosylation of RyR.
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