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Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation.


ABSTRACT: Cysteine S-nitrosylation is a posttranslational modification by which nitric oxide regulates protein function and signaling. Studies of individual proteins have elucidated specific functional roles for S-nitrosylation, but knowledge of the extent of endogenous S-nitrosylation, the sites that are nitrosylated, and the regulatory consequences of S-nitrosylation remains limited. We used mass spectrometry-based methodologies to identify 1011 S-nitrosocysteine residues in 647 proteins in various mouse tissues. We uncovered selective S-nitrosylation of enzymes participating in glycolysis, gluconeogenesis, tricarboxylic acid cycle, and oxidative phosphorylation, indicating that this posttranslational modification may regulate metabolism and mitochondrial bioenergetics. S-nitrosylation of the liver enzyme VLCAD [very long chain acyl-coenzyme A (CoA) dehydrogenase] at Cys(238), which was absent in mice lacking endothelial nitric oxide synthase, improved its catalytic efficiency. These data implicate protein S-nitrosylation in the regulation of ?-oxidation of fatty acids in mitochondria.

SUBMITTER: Doulias PT 

PROVIDER: S-EPMC4010156 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation.

Doulias Paschalis-Thomas PT   Tenopoulou Margarita M   Greene Jennifer L JL   Raju Karthik K   Ischiropoulos Harry H  

Science signaling 20130101 256


Cysteine S-nitrosylation is a posttranslational modification by which nitric oxide regulates protein function and signaling. Studies of individual proteins have elucidated specific functional roles for S-nitrosylation, but knowledge of the extent of endogenous S-nitrosylation, the sites that are nitrosylated, and the regulatory consequences of S-nitrosylation remains limited. We used mass spectrometry-based methodologies to identify 1011 S-nitrosocysteine residues in 647 proteins in various mous  ...[more]

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