Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling

Skoko, John; Attaran, Shireen; Neumann, Carola

doi:10.3390/antiox8020029

Title: Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling

Journal Article · 23 January 2019 · Antioxidants

DOI: https://doi.org/10.3390/antiox8020029 · OSTI ID:1560587

Skoko, John ^[1]; Attaran, Shireen ^[1]; Neumann, Carola ^[1]

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.

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.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1560587

Journal Information:: Antioxidants, Vol. 8, Issue 2; ISSN 2076-3921

Publisher:: MDPICopyright Statement

Country of Publication:: United States

Language:: English

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Quantitative phosphoproteomic analysis reveals system-wide signaling pathways downstream of SDF-1/CXCR4 in breast cancer stem cells Yi, T.; Zhai, B.; Yu, Y. Proceedings of the National Academy of Sciences, Vol. 111, Issue 21 https://doi.org/10.1073/pnas.1404943111	journal	April 2014
Phosphoproteomic differences in major depressive disorder postmortem brains indicate effects on synaptic function Martins-de-Souza, Daniel; Guest, Paul C.; Vanattou-Saifoudine, Natacha European Archives of Psychiatry and Clinical Neuroscience, Vol. 262, Issue 8 https://doi.org/10.1007/s00406-012-0301-3	journal	February 2012
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