期刊
SCIENCE ADVANCES
卷 6, 期 1, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aax8358
关键词
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资金
- 2019 Hungarian Thematic Excellence Program [TUDFO/51757/2019-ITM]
- Hungarian National Research, Development and Innovation Office [KH_126766, K_129286, PD_132082]
- Japan Society for the Promotion of Science [L19520]
- Ministry of Education, Culture, Sports, Science and Technology of Japan [17H05519, 17K15489]
- Ministry of Education, Sciences, Sports, and Technology (MEXT), Japan [18H05277, 26111001, 15K21759, 17K08619, 17K15408]
- Karolinska Institutet
- Swedish Research Council [2013-765, 2014-2603, 2017-01872, 537-2014-360]
- Swedish Cancer Society [2015/238, 2018/333]
- Knut and Alice Wallenberg Foundations [KAW 2015.0063]
- Swedish Foundation for International Cooperation in Research and Higher Education (STINT) [JA2018-7581]
- Swedish Society of Medicine [SLS-786841]
- Ake Wiberg Stiftelse [M17-0101, M18-0141]
- U.S. NIH [OD026444, AG040020, GM110732, AG055022, CA215784]
- Montana/Interstate Agricultural Experiment Station [MONB00443, W4171]
- Montana State University Department of Microbiology
- Swedish Research Council [2017-01872] Funding Source: Swedish Research Council
- Grants-in-Aid for Scientific Research [17K08619, 17K15408, 17H05519, 26111001, 18H05277, 17K15489, 15K21759] Funding Source: KAKEN
Irreversible oxidation of Cys residues to sulfinic/sulfonic forms typically impairs protein function. We found that persulfidation (CysSSH) protects Cys from irreversible oxidative loss of function by the formation of CysSSO(1-3)H derivatives that can subsequently be reduced back to native thiols. Reductive reactivation of oxidized persulfides by the thioredoxin system was demonstrated in albumin, Prx2, and PTP1B. In cells, this mechanism protects and regulates key proteins of signaling pathways, including Prx2, PTEN, PTP1B, HSP90, and KEAP1. Using quantitative mass spectrometry, we show that (i) CysSSH and CysSSO(3)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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