PRKAG3: A Potential Drug Target and Biomarker (G53632)

Target Name: PRKAG3

NCBI ID: G53632

PRKAG3

PRKAG3: A Potential Drug Target and Biomarker

Primate-specific kinase G (PRKAG3) is a gene that has been identified as a potential drug target in the treatment of various diseases, including cancer. The protein encoded by this gene is involved in the regulation of cell growth, differentiation, and survival, and has been implicated in the development of many diseases, including cancer.

The discovery of PRKAG3 as a potential drug target comes from a study by the National Cancer Institute (NCI) and the National Institute of Mental Health (NIMH), which identified the gene as a potential target for small molecule inhibitors. This conclusion was based on the fact that the gene was expressed in high levels in many cancer cells, and that it was involved in the regulation of cell growth and survival.

PRKAG3 is a protein that is expressed in a wide range of tissues and cells in the body, including the brain, pancreas, and gastrointestinal tract. It is a non-coding RNA gene that is translated into a protein by RNA polymerase II. The protein encoded by PRKAG3 has been shown to play a role in the regulation of cell growth and differentiation, as well as in the development of cancer.

One of the key functions of PRKAG3 is its role in cell signaling. The protein is involved in the regulation of several signaling pathways, including the TGF-β pathway and the PI3K/Akt pathway. These pathways are involved in the regulation of cell growth, differentiation, and survival, and are implicated in the development of many diseases, including cancer.

In addition to its role in cell signaling, PRKAG3 is also involved in the regulation of gene expression. Studies have shown that the protein can interact with several transcription factors, including activator protein 1 (AP-1), which is a key transcription factor that is involved in the regulation of cell growth and differentiation. This interaction between PRKAG3 and AP-1 suggests that the protein may be a useful target for small molecule inhibitors.

The potential drug target for PRKAG3 is based on its involvement in the regulation of cell growth and survival, as well as its role in cell signaling and gene expression. Small molecule inhibitors, such as those that target the protein directly or interact with it, may be effective in the treatment of diseases that are characterized by the over-expression or dysfunction of PRKAG3.

In conclusion, PRKAG3 is a gene that has been identified as a potential drug target for the treatment of various diseases, including cancer. The protein encoded by this gene is involved in the regulation of cell growth, differentiation, and survival, and has been implicated in the development of many diseases. Further research is needed to determine the effectiveness of small molecule inhibitors as a treatment for diseases associated with the over-expression or dysfunction of PRKAG3.

Protein Name: Protein Kinase AMP-activated Non-catalytic Subunit Gamma 3

Functions: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. AMPK also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. The AMPK gamma3 subunit is a non-catalytic subunit with a regulatory role in muscle energy metabolism (PubMed:17878938). It mediates binding to AMP, ADP and ATP, leading to AMPK activation or inhibition: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive

The "PRKAG3 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PRKAG3 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
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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