Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling
Abstract
Reactive oxygen and nitrogen species have cell signaling properties and are involved in a multitude of processes beyond redox homeostasis. The peroxiredoxin (Prdx) proteins are highly sensitive intracellular peroxidases that can coordinate cell signaling via direct reactive species scavenging or by acting as a redox sensor that enables control of binding partner activity. Oxidation of the peroxidatic cysteine residue of Prdx proteins are the classical post-translational modification that has been recognized to modulate downstream signaling cascades, but increasing evidence supports that dynamic changes to phosphorylation of Prdx proteins is also an important determinant in redox signaling. Phosphorylation of Prdx proteins affects three-dimensional structure and function to coordinate cell proliferation, wound healing, cell fate and lipid signaling. The advent of large proteomic datasets has shown that there are many opportunities to understand further how phosphorylation of Prdx proteins fit into intracellular signaling cascades in normal or malignant cells and that more research is necessary. This review summarizes the Prdx family of proteins and details how post-translational modification by kinases and phosphatases controls intracellular signaling.
- Authors:
-
- Univ. of Pittsburgh, Pittsburgh, PA (United States). Dept. of Pharmacology and Chemical Biology, School of Medicine; Univ. of Pittsburgh, Pittsburgh, PA (United States). Medical Center Hillman Cancer Center, Women’s Cancer Research Center; Magee-Women’s Hospital of UPMC, Pittsburgh, PA (United States). Magee-Women’s Research Inst.
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1560587
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Antioxidants
- Additional Journal Information:
- Journal Volume: 8; Journal Issue: 2; Journal ID: ISSN 2076-3921
- Publisher:
- MDPI
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; peroxiredoxin; Prdx; Prx; redox signaling; cell signaling; phosphorylation
Citation Formats
Skoko, John, Attaran, Shireen, and Neumann, Carola. Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling. United States: N. p., 2019.
Web. doi:10.3390/antiox8020029.
Skoko, John, Attaran, Shireen, & Neumann, Carola. Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling. United States. https://doi.org/10.3390/antiox8020029
Skoko, John, Attaran, Shireen, and Neumann, Carola. Wed .
"Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling". United States. https://doi.org/10.3390/antiox8020029. https://www.osti.gov/servlets/purl/1560587.
@article{osti_1560587,
title = {Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling},
author = {Skoko, John and Attaran, Shireen and Neumann, Carola},
abstractNote = {Reactive oxygen and nitrogen species have cell signaling properties and are involved in a multitude of processes beyond redox homeostasis. The peroxiredoxin (Prdx) proteins are highly sensitive intracellular peroxidases that can coordinate cell signaling via direct reactive species scavenging or by acting as a redox sensor that enables control of binding partner activity. Oxidation of the peroxidatic cysteine residue of Prdx proteins are the classical post-translational modification that has been recognized to modulate downstream signaling cascades, but increasing evidence supports that dynamic changes to phosphorylation of Prdx proteins is also an important determinant in redox signaling. Phosphorylation of Prdx proteins affects three-dimensional structure and function to coordinate cell proliferation, wound healing, cell fate and lipid signaling. The advent of large proteomic datasets has shown that there are many opportunities to understand further how phosphorylation of Prdx proteins fit into intracellular signaling cascades in normal or malignant cells and that more research is necessary. This review summarizes the Prdx family of proteins and details how post-translational modification by kinases and phosphatases controls intracellular signaling.},
doi = {10.3390/antiox8020029},
journal = {Antioxidants},
number = 2,
volume = 8,
place = {United States},
year = {2019},
month = {1}
}
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Figure 1: Reduction of H2O2 by typical 2-Cys Prdx. H2O2 recycling by 2-Cys typical Prdx family members involves the conversion of the peroxidatic Cys to sulfenic acid. Sulfenylated Prdx protein can then either form a disulfide bond with the resolving Cys on the dimeric partner protein to be recycled viamore »
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Works referencing / citing this record:
Redox Signaling from Mitochondria: Signal Propagation and Its Targets
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- Ježek, Petr; Holendová, Blanka; Plecitá-Hlavatá, Lydie
- Biomolecules, Vol. 10, Issue 1
Figures/Tables have been extracted from DOE-funded journal article accepted manuscripts.