Control of protein function through oxidation and reduction of persulfidated states
Éva Dóka(National Institute of Oncology), Tomoaki Ida(Tohoku University), Markus Dagnell(Karolinska Institutet), Yumi Abiko(University of Tsukuba), Nho Cong Luong(University of Tsukuba), Noémi Balog(National Institute of Oncology), Tsuyoshi Takata(Tohoku University), Belén Espinosa(Karolinska Institutet), Akira Nishimura(Tohoku University), Qing Cheng(Karolinska Institutet), Yosuke Funato(The University of Osaka), Hiroaki Miki(The University of Osaka), Jon M. Fukuto(Sonoma State University), Justin R. Prigge(Montana State University), Edward E. Schmidt(Montana State University), Elias S.J. Arnér(Karolinska Institutet), Yoshito Kumagai(University of Tsukuba), Takaaki Akaike(Tohoku University), Péter Nagy(National Institute of Oncology)
Cited by 209Open Access
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.
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