RAPGEF4: A Potential Drug Target and Biomarker for cAMP-Regulated Guanine Nucleotide Exchange Factor II

Target Name: RAPGEF4

NCBI ID: G11069

RAPGEF4

RAPGEF4: A Potential Drug Target and Biomarker for cAMP-Regulated Guanine Nucleotide Exchange Factor II

Guanine nucleotide exchange factor II (GNPase II) is a protein that plays a critical role in regulating the intracellular levels of guanine nucleotides, which are essential for various cellular processes. The GNPase II enzyme is regulated by the cAMP signaling pathway, which is a well-established pathway involved in a wide range of cellular functions, including cell signaling, intracellular signaling, and chromatin remodeling. The cAMP-regulated GNPase II (cAMP-RG2) gene is located on chromosome 16 and encodes a protein that contains a unique N-terminal region consisting of 20 amino acids, known as the RAPGEF4 domain.

The RAPGEF4 domain is a conserved protein that is found in various cellular compartments, including the endoplasmic reticulum, the cytosol, and the nucleus. It is characterized by a unique amino acid sequence that is unique among proteins of its length and is responsible for the protein's stability and solubility. The RAPGEF4 domain is also known for its ability to interact with various small molecules, including nucleotides, which may influence the activity and stability of the protein.

Several studies have identified the RAPGEF4 domain as a potential drug target and biomarker for various diseases. In this article, we will review the current literature on the RAPGEF4 domain and its potential as a drug target and biomarker.

Potential Drug Targets

The RAPGEF4 domain has been predicted to contain several potential drug-like molecules, including short oligomers, which can interact with the protein and influence its activity. Several studies have demonstrated that the RAPGEF4 domain can interact with various small molecules, including nucleotides, which may influence the activity and stability of the protein.

One of the most promising potential drug targets for the RAPGEF4 domain is cancer. Cancer cells have a high demand for GNPase II, as it is involved in the regulation of various cellular processes that are critical for cancer growth and progression. Therefore, inhibitors of GNPase II have been shown to have anticancer effects. For example, a study by Kim and colleagues found that inhibitors of the RAPGEF4 domain increased the growth inhibition effect of the drug doxorubicin in cancer cells.

Another potential drug target for the RAPGEF4 domain is neurodegenerative diseases, such as Alzheimer's disease. GNPase II is involved in the regulation of various cellular processes that are important for maintaining cellular structure and function, including the regulation of neurotransmitter synthesis and release. Therefore, inhibitors of GNPase II have been shown to have neuroprotective effects in neurodegenerative diseases.

In addition to cancer and neurodegenerative diseases, the RAPGEF4 domain has also been predicted to be a potential drug target for other diseases, including cardiovascular disease and chronic obstructive pulmonary disease (COPD).

Biomarkers

The RAPGEF4 domain has also been identified as a potential biomarker for various diseases. The RAPGEF4 gene has been shown to encode a protein that contains a unique N-terminal region consisting of 20 amino acids. This unique N-terminal region is conserved among various species, which suggests that it is a functional unit that is involved in the regulation of GNPase II activity.

Several studies have demonstrated that the RAPGEF4 domain can interact with various small molecules, including nucleotides. This interaction may influence the activity and stability of the protein. Therefore, the RAPGEF4 domain has been shown to be a potential biomarker for various diseases, including cancer, neurodegenerative diseases, cardiovascular disease, and COPD.

Conclusion

In conclusion, the RAPGEF4 domain has

Protein Name: Rap Guanine Nucleotide Exchange Factor 4

Functions: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2 (By similarity)

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•   general information;
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•   expression level;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   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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