P043. S-nitrosylation of Hsp90 and its relationship with eNOS: A negative feedback loop in the NO-producing system?

Identification of Protein Targets of S-Nitroso-Coenzyme A-Mediated S-Nitrosation Using Chemoproteomics

“…15 Some well-characterized targets of S-nitrosation include caspase 3 (Casp3) 16 and heat shock protein 90 (Hsp90). 17 Constitutive S-nitrosation of the active-site Cys163 on Casp3 prevents cleavage of the procaspase to its active form, inhibiting protease activity and suppressing the apoptotic pathway. 16 Cys521 on the molecular chaperone Hsp90 serves as a conformational switch, where S-nitrosation disrupts interaction with Hsp90/activator of Hsp90 ATPase activity 1 (AHA1), inhibiting ATPase activity and promoting interaction with the cell division cycle 37 protein (CDC37) to activate subsequent NF-κB signaling.…”

“…16 Cys521 on the molecular chaperone Hsp90 serves as a conformational switch, where S-nitrosation disrupts interaction with Hsp90/activator of Hsp90 ATPase activity 1 (AHA1), inhibiting ATPase activity and promoting interaction with the cell division cycle 37 protein (CDC37) to activate subsequent NF-κB signaling. 17,18 Because S-nitrosation can impart such diverse effects on target proteins, determining the precise modification sites and functional impacts of individual cysteine S-nitrosation events is crucial to fully understanding the role of this modification in biological processes.…”