Control of protein function through oxidation and reduction of persulfidated states
Éva Dóka, Tomoaki Ida, Markus Dagnell, Yumi Abiko, Nho Cong Luong, Noémi Balog, Tsuyoshi Takata, Belén Espinosa, Akira Nishimura, Qing Cheng, Yosuke Funato, Hiroaki Miki, Jon M. Fukuto, Justin R. Prigge, Edward E. Schmidt, Elias S.J. Arnér, Yoshito Kumagai, Takaaki Akaike, Péter Nagy
Abstract
H species are abundant in mouse liver and enzymatically regulated by the glutathione and thioredoxin systems and (ii) deletion of the thioredoxin-related protein TRP14 in mice altered CysSSH levels on a subset of proteins, predicting a role for TRP14 in persulfide signaling. Furthermore, selenium supplementation, polysulfide treatment, or knockdown of TRP14 mediated cellular responses to EGF, suggesting a role for TrxR1/TRP14-regulated oxidative persulfidation in growth factor responsiveness.