Asset Details
Do you wish to reserve the book?
Oxidative Stress Orchestrates MAPK and Nitric-Oxide Synthase Signal
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Oxidative Stress Orchestrates MAPK and Nitric-Oxide Synthase Signal
Do you wish to request the book?
Oxidative Stress Orchestrates MAPK and Nitric-Oxide Synthase Signal
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Oxidative Stress Orchestrates MAPK and Nitric-Oxide Synthase Signal
2020
Overview
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.
Publisher
MDPI AG,MDPI
Subject
/ Animals
/ Calcium-Calmodulin-Dependent Protein Kinase Type 1 - genetics
/ Calcium-Calmodulin-Dependent Protein Kinase Type 1 - metabolism
/ Calcium-Calmodulin-Dependent Protein Kinase Type 2 - genetics
/ Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism
/ Humans
/ Huntington Disease - enzymology
/ Huntington Disease - genetics
/ Huntington Disease - pathology
/ Kinases
/ Nitric Oxide Synthase Type I - genetics
/ Nitric Oxide Synthase Type I - metabolism
/ Protein Processing, Post-Translational
/ Proteins
/ Reactive Oxygen Species - metabolism
/ Review
/ Ribosomal Protein S6 Kinases, 90-kDa - genetics
