PPP3R2: A Potential Drug Target and Biomarker for Protein Phosphatase 3 Regulatory Subunit B Beta Isoform

Target Name: PPP3R2

NCBI ID: G5535

PPP3R2

PPP3R2: A Potential Drug Target and Biomarker for Protein Phosphatase 3 Regulatory Subunit B Beta Isoform

Protein phosphatase 3 (PPP3) is an essential enzyme in the PI3K/AKT signaling pathway that regulates various cellular processes, including cell survival, metabolism, and inflammation. The PPP3 regulatory subunit B (PPP3R2) is a key protein that interacts with PPP3 and plays a critical role in its function. However, its role in the regulation of cellular processes is not well understood, and it remains an attractive target for drug development. In this article, we will discuss the potential drug target and biomarker for PPP3R2, focusing on its function and current research in the field.

Function of PPP3R2

PPP3R2 is a 21-kDa protein that contains a N-terminal kinase domain, a catalytic domain, and a C-terminal regulatory domain. The N-terminal kinase domain is responsible for the kinetic activity of PPP3R2, while the catalytic domain catalyzes the dephosphorylation of PPP3, which is the rate-limiting step in the PPP3 signaling pathway. The C-terminal regulatory domain is responsible for regulating the activity of PPP3R2 and interacting with various cellular signaling pathways, including the PI3K/AKT signaling pathway, the TOR signaling pathway, and the NF-kappa-B signaling pathway.

In the PI3K/AKT signaling pathway, PPP3R2 plays a crucial role in regulating the activity of PPP3. It has been shown that PPP3R2 is a negative regulator of PPP3, which means that it promotes the dephosphorylation of PPP3 at the expense of its own phosphorylation. This regulatory mechanism allows for the inhibition of the negative feedback loop that regulates the activity of PPP3, leading to increased signaling activity and the promotion of cellular processes such as cell survival, metabolism, and angiogenesis.

PPP3R2 has also been shown to play a role in the regulation of cellular apoptosis. Studies have shown that PPP3R2 can induce cell apoptosis in various cellular models, including cancer cells, and that its activity is regulated by various factors, including the expression level of PPP3R2, the phosphorylation state of PPP3, and the presence of inhibitors. These findings highlight the potential of PPP3R2 as a drug target for cancer treatment.

Current Research

The drug targeting of PPP3R2 has been the focus of extensive research in recent years, with several studies investigating its potential as a therapeutic agent. One of the main challenges in the development of PPP3R2-based drugs is the lack of understanding of its precise mechanism of action and the complexity of its regulation. To overcome this challenge, researchers have used various techniques, including biochemical, cellular, and in vitro studies, to gain insight into the function of PPP3R2.

One of the most significant findings of recent research is the identification of a new regulatory interaction between PPP3R2 and PPP3. Studies have shown that PPP3R2 can interact with a conformational variation of PPP3, which is caused by the presence of a unique phosphoryl group at its N-terminus. This interaction between PPP3R2 and PPP3 has important implications for the regulation of PPP3 signaling pathways, including the regulation of cell growth, metabolism, and angiogenesis.

Another promising area of research is the study of the role of PPP3R2 in the regulation of cellular apoptosis. Studies have shown that PPP3R2 can

Protein Name: Protein Phosphatase 3 Regulatory Subunit B, Beta

Functions: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity

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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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