SMURF2: A Potential Drug Target and Biomarker (G64750)

Target Name: SMURF2

NCBI ID: G64750

SMURF2

SMURF2: A Potential Drug Target and Biomarker

SMAD-specific E3 ubiquitin-protein ligase 2 (SMURF2) is a protein that plays a crucial role in cell signaling pathways. It is a key enzyme in the ubiquitin-protein ligase (UPL) system, which is responsible for the degradation of damaged or unnecessary proteins. Mutations in the SMURF2 gene have been linked to various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Therefore, targeting SMURF2 has the potential to be a valuable drug target and biomarker.

SMURF2 is a 21-kDa protein that is expressed in various tissues, including liver, pancreas, and muscle. It is a member of the SMAD family of proteins, which includes SMAD1, SMAD4, and SMAD5. The SMAD family of proteins are known for their ability to recognize and ubiquitinate specific protein targets. SMURF2 is specifically involved in the degradation of Ubiquitin (U) proteins, which are involved in various cellular processes, including cell signaling, DNA damage repair, and inflammation.

SMURF2 functions as an enzyme that adds a ubiquitin tag to specific target proteins. This ubiquitin tag is attached to the target protein, which can interact with other proteins and influence various cellular processes. The addition of the ubiquitin tag to the target protein is a critical step in the UPL system, as it allows the target protein to be degraded by the ubiquitin-protein ligase.

SMURF2 is also involved in the regulation of protein stability and quality control. It has been shown to play a role in the degradation of damaged or misfolded proteins, which can contribute to the development of neurodegenerative diseases. Additionally, SMURF2 has been linked to the regulation of protein synthesis and degradation in various cellular processes, including cell signaling, DNA damage repair, and inflammation.

SMURF2 has also been shown to be involved in the regulation of cell adhesion and migration. It has been shown to play a role in the degradation of adhesion molecules, such as cadherins and E-cadherins, which are involved in cell-cell adhesion. This suggests that SMURF2 may be involved in the regulation of cell-cell adhesion and the development of various diseases, including cancer.

In addition to its role in cell signaling and protein regulation, SMURF2 has also been shown to be involved in the development of certain diseases. Mutations in the SMURF2 gene have been linked to various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, studies have shown that mutations in the SMURF2 gene are associated with the development of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Additionally, SMURF2 has been shown to play a role in the development of certain autoimmune disorders, such as rheumatoid arthritis and multiple sclerosis.

Targeting SMURF2 as a drug target has the potential to be a valuable treatment for a variety of diseases. By inhibiting the activity of SMURF2, researchers may be able to reduce the production of damaged or misfolded proteins and improve the stability and quality of remaining proteins. This could lead to a reduction in the development of neurodegenerative diseases, cancer, and autoimmune disorders.

In addition to its potential as a drug target, SMURF2 also has the potential as a biomarker. The degradation of specific proteins by SMURF2 can be used as a marker for the diagnosis and monitoring of various diseases. For example, the degradation of Ubiquitin proteins by SMURF2 can be used as a marker for the diagnosis of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Additionally, the degradation of certain proteins by SMURF2 can be used as a marker for the diagnosis of certain autoimmune disorders, such as rheumatoid arthritis and multiple sclerosis.

In conclusion, SMURF2 is a protein that plays a crucial role in

Protein Name: SMAD Specific E3 Ubiquitin Protein Ligase 2

Functions: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11016919). Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling (PubMed:11163210, PubMed:12717440, PubMed:21791611). In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1 (PubMed:18448069). Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation (PubMed:11016919, PubMed:11158580, PubMed:11389444). SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation (PubMed:11389444). Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation (PubMed:30696809)

The "SMURF2 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 SMURF2 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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