Guanine Nucleotide Binding Protein GNAT3: Potential Therapeutic Targets and Biomarker for Various Diseases

Target Name: GNAT3

NCBI ID: G346562

GNAT3

Guanine Nucleotide Binding Protein GNAT3: Potential Therapeutic Targets and Biomarker for Various Diseases

Guanine nucleotide binding proteins (GNATPs) are a family of proteins that play a crucial role in gene regulation. They are involved in the regulation of DNA binding and translation of RNA in various organisms, including humans. GNATPs are composed of two main domains: an alpha transducing region and a beta-sheet domain. The alpha transducing region is responsible for binding to DNA and transmitting genetic information to the cell's RNA machinery.

Guanine nucleotide binding proteins have been implicated in various diseases, including cancer, neurodegenerative diseases, and developmental disorders. Therefore, there is a growing interest in developing drugs that target GNATPs as a potential therapeutic approach. In this article, we will explore GNAT3, a protein that is known to be a drug target and a potential biomarker for various diseases.

Structure and Function

GNAT3 is a 21-kDa protein that is composed of 215 amino acid residues. It has a characteristic alpha-helices structure and a distinct beta-sheet domain. The alpha-helices are responsible for the protein's stability and function.

The alpha transducing region is the most conserved domain in GNATPs. It is composed of 136 amino acid residues and is responsible for binding to DNA. The alpha-helices in this region are responsible for transmitting genetic information to the cell's RNA machinery. GNAT3 has been shown to play a role in the regulation of gene expression, including the regulation of cell adhesion and the development of cancer.

The beta-sheet domain is the least conserved domain in GNATPs. It is composed of 34 amino acid residues and is responsible for the protein's stability. The beta-sheet domain is known for its role in protein-protein interactions and has been implicated in GNAT3's stability and function.

Expression and Function

GNAT3 is expressed in various tissues and cells in the body. It is highly expressed in the brain, heart, and testes, and is also expressed in the liver, pancreas, and placenta. GNAT3 has been shown to play a role in the regulation of gene expression in these tissues.

In addition to its expression in tissues, GNAT3 has also been shown to play a role in the regulation of DNA binding and translation in various organisms. GNAT3 has been shown to interact with various DNA-binding proteins, including the DNA-binding domain of the RNA polymerase II (RNA-P2). This interaction between GNAT3 and RNA-P2 suggests that GNAT3 may be involved in the regulation of gene expression by binding to DNA and transmitting genetic information to the cell's RNA machinery.

Drug Targeting

GNAT3 is a drug target of interest in various diseases, including cancer, neurodegenerative diseases, and developmental disorders. Several studies have shown that inhibiting GNAT3 can be effective in treating these diseases.

For example, studies have shown that inhibiting GNAT3 can be effective in treating neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. In these diseases, the accumulation of misfolded proteins and neurofibrillary tangles is thought to contribute to the progression of the disease. GNAT3 has been shown to play a role in the regulation of misfolded protein formation and may be a potential therapeutic target for these diseases.

In addition to its potential use in neurodegenerative diseases, GNAT3 has also been shown to be involved in the regulation of cancer development. Studies have shown that GNAT3 can be involved in the regulation of cell cycle progression and the maintenance of stem cell properties. Therefore, GNAT3 may be a potential therapeutic target for cancer.

Biomarker

GNAT3 may also be a useful biomarker for various diseases, including cancer. The expression of GNAT3 has been shown to be associated with the development

Protein Name: G Protein Subunit Alpha Transducin 3

Functions: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity

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