Target Name: Membrane-Bound Protein Tyrosine Phosphatases (rPTPs)
NCBI ID: P43165
Review Report on Membrane-Bound Protein Tyrosine Phosphatases (rPTPs)  Target / Biomarker Content of Review Report on Membrane-Bound Protein Tyrosine Phosphatases (rPTPs)  Target / Biomarker
Membrane-Bound Protein Tyrosine Phosphatases (rPTPs)
Other Name(s): R-PTP | rPTP

rPTPs: Versatile Regulators of Cellular Signaling and Metabolism

Membrane-bound protein tyrosine phosphatases (rPTPs), also known as nonspecific subtype (R-PTP), are a family of enzymes that play a crucial role in cellular signaling and metabolism. These enzymes belong to the protein tyrosine phosphatase (PTP) superfamily, which is a large and diverse group of enzymes that regulate protein tyrosination and phosphorylation.

rPTPs are widely distributed throughout various cellular compartments, including the cytoplasm, the endoplasmic reticulum, the mitochondria, and the endoplasmic reticulum. They are involved in the regulation of a variety of cellular processes, including cell signaling, DNA replication, and protein transport.

One of the key functions of rPTPs is to regulate protein tyrosination, which is the process by which tyrosine residues on proteins are added with a phosphate group. This process is critical for the regulation of cellular signaling pathways, as tyrosination is often associated with the activation of protein kinases and other signaling pathways.

In addition to their role in protein tyrosination, rPTPs are also involved in the regulation of protein phosphorylation, which is the process by which proteins are added with a phosphate group. This process is critical for the regulation of protein stability, localization, and interactions with other cellular components.

rPTPs are a subset of the PTP superfamily, which includes several different subtypes, including the classic PTP (PTP1), the catalytic subtype (PTP2), and the regulatory subtype (PTP3). These subtypes differ in their catalytic activity, as well as their subcellular localization and stability.

One of the key features of rPTPs is their ability to localize to specific cellular compartments and to interact with specific protein substrates. This allows them to play important roles in the regulation of cellular processes, including the regulation of cell signaling pathways and the regulation of protein transport.

In recent years, the study of rPTPs has gained significant interest, as these enzymes have been identified as potential drug targets and biomarkers. The use of small molecule inhibitors to selectively inhibit rPTP activity has been shown to be effective in a variety of cellular contexts, including the regulation of cancer growth and the treatment of neurodegenerative diseases.

In addition to their potential as drug targets, rPTPs are also widely studied as potential biomarkers for a variety of cellular processes, including the regulation of cell signaling pathways and the regulation of protein transport. The use of RNA assays and other techniques has allowed researchers to identify and quantify rPTP activity in a variety of cellular contexts, including the cytoplasm and the endoplasmic reticulum.

Overall, the study of rPTPs is an important area of research, as these enzymes play critical roles in the regulation of cellular processes and are potential drug targets and biomarkers. Further studies are needed to fully understand the mechanisms of rPTP activity and their role in cellular signaling and metabolism.

Protein Name: Membrane-Bound Protein Tyrosine Phosphatases (rPTPs) (nonspecified Subtype)

The "Membrane-Bound Protein Tyrosine Phosphatases (rPTPs) 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 Membrane-Bound Protein Tyrosine Phosphatases (rPTPs) 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

More Common Targets

Membrane-spanning 4-domains subfamily A member 4A | MEMO1 | MEMO1P1 | MEMO1P4 | MEMO1P5 | MEN1 | MEOX1 | MEOX2 | MEP1A | MEP1AP2 | MEP1AP4 | MEP1B | MEPCE | MEPE | MERTK | MESD | MESP1 | MESP2 | MEST | MESTIT1 | MESTP3 | MESTP4 | MET | Metabotropic glutamate (mGluR) receptor | Metallothionein | METAP1 | METAP1D | METAP2 | Metaxin complex | Methionine adenosyltransferase | Methionine adenosyltransferase II | Methionyl aminopeptidase | Methylcytosine dioxygenase (TET) | METRN | METRNL | METTL1 | METTL13 | METTL14 | METTL15 | METTL15P1 | METTL15P2 | METTL16 | METTL17 | METTL18 | METTL21A | METTL21C | METTL21EP | METTL22 | METTL23 | METTL24 | METTL25 | METTL25B | METTL26 | METTL27 | METTL2A | METTL2B | METTL3 | METTL4 | METTL5 | METTL6 | METTL7A | METTL7B | METTL8 | METTL9 | MEX3A | MEX3B | MEX3C | MEX3D | MFAP1 | MFAP2 | MFAP3 | MFAP3L | MFAP4 | MFAP5 | MFF | MFF-DT | MFGE8 | MFHAS1 | MFN1 | MFN2 | MFNG | MFRP | MFSD1 | MFSD10 | MFSD11 | MFSD12 | MFSD13A | MFSD14A | MFSD14B | MFSD14CP | MFSD2A | MFSD2B | MFSD3 | MFSD4A | MFSD4A-AS1 | MFSD4B | MFSD4B-DT | MFSD5 | MFSD6 | MFSD6L