Vie de l'IBPC


Séminaire UMR8226



Hong Li - Regulation of NO-dependent Proteins Modifications in Mammalian Cells

Regulation of NO-dependent Proteins Modifications
in Mammalian Cells

Hong Li

 Center for Advanced Proteomics Research
Department of Microbiology, Biochemistry and Molecular Genetics
Rutgers University - New Jersey Medical School, USA

invité  par Stéphane Lemaire et Christophe Marchand

le lundi 8  janvier 2018 à 11h - Salle de conférence de l'IBPC - 3e étage



Nitric oxide (NO) is best known for its ability to stimulate soluble guanylyl cyclase (sGC) to produce cGMP and stimulate downstream signaling pathways. However, NO can also covalently modify cysteines via S-nitrosation (addition of a NO moiety to the cysteine of a protein, SNO) and modulate other redox thiol modifications. Although S-nitrosation is increasingly recognized as an important regulatory mechanism of protein function, and to play a role in cardiac protection, dynamic regulation of protein nitrosation specificity is poorly understood. Our collaborative team has made an exciting observation that sGC, the key NO receptor, modulates the level of nitrosation of specific proteins in cardiomyocytes. This novel observations lead to the idea that sGC modulates S-nitrosation specificity via a transnitrosation cascade that includes key S-nitrosated intermediates. This project could lead to the discovery of novel cardioprotective pathways driven by specific S-nitrosation, and downstream disulfide bond reconfigurations.
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