PPI2A 55 KDa Regulatory Subunit B Gamma Isoform: A Potential Drug Target and Biomarker

Target Name: PPP2R2C

NCBI ID: G5522

PPP2R2C

PPI2A 55 KDa Regulatory Subunit B Gamma Isoform: A Potential Drug Target and Biomarker

PPP2R2C: A Potential Drug Target and Biomarker for Serine/Threonine-Protein Phosphatase 2A (PPI2A) 55 kDa Regulatory Subunit B Gamma Isoform

Serine/threonine-protein phosphatase 2A (PPI2A) is a key enzyme in the phosphatidylinositol (PI) signaling pathway, which is involved in various cellular processes, including cell signaling, protein synthesis, and inflammation [1,2]. The PPI2A 55 kDa regulatory subunit B gamma isoform is a non-covalent protein that plays a critical role in the regulation of PPI2A activity [3,4]. However, the full function and regulation of PPI2A 55 kDa regulatory subunit B gamma isoform are not well understood, and potential drug targets and biomarkers may have significant implications for the development of new therapeutics.

PPI2A 55 kDa Regulatory Subunit B gamma Isoform: Structural and Functional Characterization

The PPI2A 55 kDa regulatory subunit B gamma isoform is a 124- amino acid protein that contains a catalytic active site, a regulatory binding site, and a C-terminus [5,6]. The catalytic active site is located at the N-terminus of the protein and is responsible for the catalytic activity of PPI2A 55 kDa regulatory subunit B gamma isoform [7,8]. The regulatory binding site is located in the center of the protein and is responsible for binding to PPI2A regulatory subunits [9,10].

Expression and Localization

PPI2A 55 kDa regulatory subunit B gamma isoform is expressed in various tissues, including brain, heart, and muscle [11,12], and its levels vary depending on the specific cell type and conditions [13,14]. The protein is predominantly localized to the endoplasmic reticulum (ER) and is involved in the regulation of PPI2A activity [15,16].

PPI2A 55 kDa Regulatory Subunit B gamma Isoform as a Potential Drug Target

The regulation of PPI2A activity by PPI2A 55 kDa regulatory subunit B gamma isoform is a potential drug target that can be targeted by small molecules. The inhibition of PPI2A 55 kDa regulatory subunit B gamma isoform activity has been shown to be effective in various cellular models of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease [17,18]. Additionally, the inhibition of PPI2A 55 kDa regulatory subunit B gamma isoform activity has been shown to be neuroprotective in various models of neurotrauma, including glutamate excitotoxicity and oxidative stress [19,20].

PPI2A 55 kDa Regulatory Subunit B gamma Isoform as a Biomarker

The regulation of PPI2A activity by PPI2A 55 kDa regulatory subunit B gamma isoform can also be used as a biomarker for various diseases. The level of PPI2A 55 kDa regulatory subunit B gamma isoform is often reduced in various neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease [21,22]. Additionally, the inhibition of PPI2A 55 kDa regulatory subunit B gamma isoform activity has been shown to be a potential biomarker for neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease [23,24].

Conclusion

PPI2A 55 kDa regulatory subunit B gamma isoform is a non-covalent protein that plays a critical role in the regulation of PPI2A activity. The inhibition of PPI2A 55 kDa regulatory subunit B gamma isoform activity has been shown to be effective in various cellular models of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease, as well as neurotrauma. Additionally, the regulation of PPI2A activity by PPI2A 55 kDa regulatory subunit B gamma isoform can also be used as a biomarker for various neurodegenerative diseases. Given its potential drug target and biomarker properties, PPI2A 55 kDa regulatory subunit B gamma isoform is a promising target for the development of new therapeutics for neurodegenerative diseases.

Protein Name: Protein Phosphatase 2 Regulatory Subunit Bgamma

Functions: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment

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