TRIM15: A Potential Drug Target for Cancer and Neurodegenerative Diseases

Target Name: TRIM15

NCBI ID: G89870

TRIM15

TRIM15: A Potential Drug Target for Cancer and Neurodegenerative Diseases

TRIM15 (TRI15_HUMAN), a protein that belongs to the TRIM family, plays a crucial role in the regulation of cell growth and differentiation. It is a key regulator of the T-cell receptor (TCR), which is responsible for cell-mediated immunity. High levels of TRIM15 have been associated with various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. As a drug target, TRIM15 has the potential to treat these diseases by modulating its activity.

The TRIM family consists of six proteins: TRIM1, TRIM2, TRIM3, TRIM4, TRIM5, and TRIM6. These proteins share a conserved N-terminal region and a conserved C-terminal region, but they differ in their lengths and their ability to regulate cell growth and differentiation. TRIM1 is the most well-studied member of the family, and it is involved in the regulation of cell growth, differentiation, and the association with the microtubules. TRIM2 and TRIM3 are involved in the regulation of mitochondrial function, while TRIM4 and TRIM6 are involved in the regulation of actin dynamics.

TRIM15 is a 19-kDa protein that is expressed in various tissues, including muscle, liver, and brain. It is primarily localized to the cytoplasm of cells and is highly stable in cell-extrusion assays. TRIM15 has been shown to interact with various cellular components, including the T-cell receptor, microtubules, and actin.

One of the most significant functions of TRIM15 is its role in regulating the T-cell receptor. The T-cell receptor is a critical signaling molecule that plays a crucial role in the regulation of immunity and inflammation. It is composed of a transmembrane domain and a cytoplasmic tail that is involved in the formation of the receptor complex. TRIM15 is known to interact with the T-cell receptor and regulate its activity.

TRIM15 has been shown to play a negative role in the regulation of T-cell receptor function. It has been shown to inhibit the phosphorylation of the T-cell receptor at its cytoplasmic tail, which is responsible for the activation of downstream signaling pathways. This inhibition of T-cell receptor signaling by TRIM15 has been shown to contribute to the immune tolerance and the regulation of autoimmune disorders.

In addition to its role in regulating T-cell receptor signaling, TRIM15 has also been shown to play a role in the regulation of cell growth and differentiation. It is a key regulator of the S-phase checkpoint, which is responsible for the regulation of DNA replication and cell growth. TRIM15 has been shown to interact with the checkpoint protein, p21, and regulate its activity.

TRIM15 has also been shown to play a role in the regulation of neurodegenerative diseases. It is a key regulator of the Parkin gene, which is involved in the development of Parkinson's disease. TRIM15 has been shown to interact with the Parkin gene and regulate its activity, which may contribute to the neurodegenerative phenotype of Parkinson's disease.

As a drug target, TRIM15 has the potential to treat various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. TRIM15 has been shown to be a potential therapeutic target in cancer, as it has been shown to inhibit the activation of the T-cell receptor at its cytoplasmic tail, which is responsible for the regulation of downstream signaling pathways. This inhibition of T-cell receptor signaling by TRIM15 has

Protein Name: Tripartite Motif Containing 15

Functions: E3 ubiquitin ligase that plays a role in several processes including innate antiviral immnity, cell migration and chemotaxis (PubMed:34142270, PubMed:23077300). Acts as a 'Lys-63'-specific ubiquitin ligase for MAPK1/ERK2 and MAPK3/ERK1, promoting their activation by facilitating their interaction with MAP2K1 and MAP2K2 (PubMed:34497368). Plays also a role in cell migration and chemotaxis by acting as a stable focal adhesion component upon recruitment by multi-adapter protein paxillin/PXN (PubMed:25015296). Functions in the RIGI-mediated interferon induction pathway upstream or at the level of MAVS (PubMed:23077300). Inhibits NF-kappa-B activation by turnover of 'Lys-63'-linked ubiquitination of MAP3K7/TAK1. Mechanistically, prevents TRIM8 cytoplasmic translocation and thus inhibits TRIM8-mediated 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 in the cytoplasm (PubMed:34871740). Plays also an important regulatory effect on the activation of hepatic stellate cells (HSCs)

The "TRIM15 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 TRIM15 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