April 1, 2003Journal of Biological ChemistryOpen Access

Compensatory Phosphorylation and Protein-Protein Interactions Revealed by Loss of Function and Gain of Function Mutants of Multiple Serine Phosphorylation Sites in Endothelial Nitric-oxide Synthase

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Population

Cells expressing endothelial nitric-oxide synthase (eNOS) mutants

Comparison

Mutation of eNOS serine phosphorylation sites to… vs Wild-type eNOS

Design

Preclinical

Authors

PBPhilip M. BauerUniversity of Louisville DFDavid FultonVascular / Pulmonary Vascular YBYong Chool BooKyungpook National University Hospital

Discussion

Member takes

Implication

Potential targets for eNOS modulation in vascular disease; leaves open in vivo translation and clinical applicability.

Structured PICO

Population

Cells expressing endothelial nitric-oxide synthase (eNOS) mutants

Intervention

Mutation of eNOS serine phosphorylation sites (116, 617, 635, 1179) to alanine (loss of function) or aspartate (gain of function)

Comparator

Wild-type eNOS

Outcome

Basal and stimulated NO release, cooperative phosphorylation, and co-association with hsp90 and Aktsurrogate

Multiple serine phosphorylation events cooperatively regulate eNOS activity, with Ser-635 and Ser-1179 acting as positive regulators and Ser-116 as a negative regulator of NO release.

Cite This Study

Bauer et al. (2003) studied this question.

synapsesocial.com/papers/6a6f24d76ceb2bbd16df9e5f https://doi.org/10.1074/jbc.m211926200

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Compensatory Phosphorylation and Protein-Protein Interactions Revealed by Loss of Function and Gain of Function Mutants of Multiple Serine Phosphorylation Sites in Endothelial Nitric-oxide Synthase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Compensatory Phosphorylation and Protein-Protein Interactions Revealed by Loss of Function and Gain of Function Mutants of Multiple Serine Phosphorylation Sites in Endothelial Nitric-oxide Synthase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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Also Consider