Abstract
Due to the growing importance of cellular signaling mediated by reactive oxygen species (ROS), proteins that are reversibly modulated by these reactant molecules are of high interest. In this context, protein kinases and phosphatases, which act coordinately in the regulation of signal transduction through the phosphorylation and dephosphorylation of target proteins, have been described to be key elements in ROS-mediated signaling events. The major mechanism by which these proteins may be modified by oxidation involves the presence of key redox-sensitive cysteine residues. Protein kinase C (PKC) is involved in a variety of cellular signaling pathways. These proteins have been shown to contain a unique structural feature that is susceptible to oxidative modification. A large number of scientific studies have highlighted the importance of ROS as a second messenger in numerous cellular processes, including cell proliferation, gene expression, adhesion, differentiation, senescence, and apoptosis. In this context, the goal of this review is to discuss the mechanisms by which PKCs are modulated by ROS and how these processes are involved in the cellular response.
Highlights
Phosphorylation, acetylation, ubiquitinylation, and glycosylation are among the most well-known post-translational modifications
The goal of this review is to discuss the mechanisms by which protein kinase Cs (PKCs) can be modulated by reactive oxygen species (ROS) and how these processes are involved in the cellular response
The PKC family is composed of serine/threonine protein kinases that are involved in a variety of pathways that regulate cell growth, differentiation, apoptosis, transformation and tumorigenicity
Summary
Phosphorylation, acetylation, ubiquitinylation, and glycosylation are among the most well-known post-translational modifications. The key elements of a signaling response are reversibility and specificity [2]. In this way, an oxidation-dependent chain reaction may be short and employ only a low concentration of oxidants to avoid irreversible damage to cellular components. Kinases and phosphatases, which act coordinately in the regulation of signal transduction through the phosphorylation and dephosphorylation of target proteins, have been described to be key elements in ROS-mediated signaling events [3,4,5,6]. The goal of this review is to discuss the mechanisms by which protein kinase Cs (PKCs) can be modulated by ROS and how these processes are involved in the cellular response. The review will focus on the structural mechanism of action of ROS in the activity of these enzymes, how ROS interact with their target molecules, the regulation of these enzymes by oxidants, and the major consequences of this tightly controlled mechanism on cell signaling
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