TY - JOUR
T1 - Multiple functions of 2-Cys peroxiredoxins, I and II, and their regulations via post-translational modifications
AU - Rhee, Sue Goo
AU - Woo, Hyun Ae
N1 - Funding Information:
This work was supported by grant from the National Research Foundation of Korea (NRF- 2015R1D1A1A01059571 ) to HAW.
Publisher Copyright:
© 2020 The Authors
PY - 2020/5/20
Y1 - 2020/5/20
N2 - Peroxiredoxins (Prxs) are an unusual family of thiol-specific peroxidases that possess a binding site for H2O2 and rely on a conserved cysteine residue for rapid reaction with H2O2. Among 6 mammalian isoforms (Prx I to VI), Prx I and Prx II are mainly found in the cytosol and nucleus. Prx I and Prx II function as antioxidant enzymes and protein chaperone under oxidative distress conditions. Under oxidative eustress conditions, Prx I and Prx II regulate the levels of H2O2 at specific area of the cells as well as sense and transduce H2O2 signaling to target proteins. Prx I and Prx II are known to be covalently modified on multiple sites: Prx I is hyperoxidized on Cys52; phosphorylated on Ser32, Thr90, and Tyr194; acetylated on Lys7, Lys16, Lys27, Lys35, and Lys197; glutathionylated on Cys52, Cys83, and Cys173; and nitrosylated on Cys52 and Cys83, whereas Prx II is hyperoxidized on Cys51; phosphorylated on Thr89, Ser112, and Thr182; acetylated on Ala2 and Lys196; glutathionylated on Cys51 and Cys172; and nitrosylated on Cys51 and Cys172. In this review, we describe how these post-translational modifications affect various functions of Prx I and Prx II.
AB - Peroxiredoxins (Prxs) are an unusual family of thiol-specific peroxidases that possess a binding site for H2O2 and rely on a conserved cysteine residue for rapid reaction with H2O2. Among 6 mammalian isoforms (Prx I to VI), Prx I and Prx II are mainly found in the cytosol and nucleus. Prx I and Prx II function as antioxidant enzymes and protein chaperone under oxidative distress conditions. Under oxidative eustress conditions, Prx I and Prx II regulate the levels of H2O2 at specific area of the cells as well as sense and transduce H2O2 signaling to target proteins. Prx I and Prx II are known to be covalently modified on multiple sites: Prx I is hyperoxidized on Cys52; phosphorylated on Ser32, Thr90, and Tyr194; acetylated on Lys7, Lys16, Lys27, Lys35, and Lys197; glutathionylated on Cys52, Cys83, and Cys173; and nitrosylated on Cys52 and Cys83, whereas Prx II is hyperoxidized on Cys51; phosphorylated on Thr89, Ser112, and Thr182; acetylated on Ala2 and Lys196; glutathionylated on Cys51 and Cys172; and nitrosylated on Cys51 and Cys172. In this review, we describe how these post-translational modifications affect various functions of Prx I and Prx II.
KW - Acetylation
KW - Chaperone
KW - Glutathionylation
KW - Hydrogen peroxide (HO)
KW - Intracellular messenger
KW - Peroxidase
KW - Peroxiredoxin
KW - Phosphorylation
KW - S-Nitrosylation
KW - Thiol oxidation
UR - http://www.scopus.com/inward/record.url?scp=85081310780&partnerID=8YFLogxK
U2 - 10.1016/j.freeradbiomed.2020.02.028
DO - 10.1016/j.freeradbiomed.2020.02.028
M3 - Review article
C2 - 32151745
AN - SCOPUS:85081310780
SN - 0891-5849
VL - 152
SP - 107
EP - 115
JO - Free Radical Biology and Medicine
JF - Free Radical Biology and Medicine
ER -