Oxidative Stress Orchestrates MAPK and Nitric-Oxide Synthase Signal

Autor: Shoma Araki, Yasuo Watanabe, Tsuyoshi Takata, Yukihiro Tsuchiya
Rok vydání: 2020
Předmět:
MAPK/ERK pathway
S-glutathionylation
Ca2+/calmodulin-dependent protein kinase (CaMK)
Nitric Oxide Synthase Type I
Review
medicine.disease_cause
lcsh:Chemistry
S-Glutathionylation
lcsh:QH301-705.5
Spectroscopy
biology
Chemistry
Kinase
nitric oxide synthase
phosphorylation
General Medicine
Glutathione
Computer Science Applications
Cell biology
Nitric oxide synthase
Huntington Disease
Oxidation-Reduction
Signal Transduction
Cell signaling
Nitric Oxide
Ribosomal Protein S6 Kinases
90-kDa
Catalysis
Inorganic Chemistry
redox regulation
Ca2+/calmodulin-dependent protein kinase
medicine
Animals
Humans
Cysteine
Physical and Theoretical Chemistry
Protein kinase A
Molecular Biology
90-kDa ribosomal S6 kinase
Organic Chemistry
Oxidative Stress
lcsh:Biology (General)
lcsh:QD1-999
Calcium-Calmodulin-Dependent Protein Kinase Type 1
biology.protein
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Reactive Oxygen Species
Protein Processing
Post-Translational
Oxidative stress
Zdroj: International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 21, Iss 8750, p 8750 (2020)
ISSN: 1422-0067
Popis: Reactive oxygen species (ROS) are not only harmful to cell survival but also essential to cell signaling through cysteine-based redox switches. In fact, ROS triggers the potential activation of mitogen-activated protein kinases (MAPKs). The 90 kDa ribosomal S6 kinase 1 (RSK1), one of the downstream mediators of the MAPK pathway, is implicated in various cellular processes through phosphorylating different substrates. As such, RSK1 associates with and phosphorylates neuronal nitric oxide (NO) synthase (nNOS) at Ser847, leading to a decrease in NO generation. In addition, the RSK1 activity is sensitive to inhibition by reversible cysteine-based redox modification of its Cys223 during oxidative stress. Aside from oxidative stress, nitrosative stress also contributes to cysteine-based redox modification. Thus, the protein kinases such as Ca2+/calmodulin (CaM)-dependent protein kinase I (CaMKI) and II (CaMKII) that phosphorylate nNOS could be potentially regulated by cysteine-based redox modification. In this review, we focus on the role of post-translational modifications in regulating nNOS and nNOS-phosphorylating protein kinases and communication among themselves.
Databáze: OpenAIRE
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