TRIM11: A Protein Regulator of Cell Division, Apoptosis and Inflammation

Target Name: TRIM11

NCBI ID: G81559

TRIM11

TRIM11: A Protein Regulator of Cell Division, Apoptosis and Inflammation

TRIM11, also known as tripartite motif containing 11, is a protein that is expressed in various tissues throughout the body. It is a key regulator of cell division and has been identified as a potential drug target in the treatment of various diseases.

The TRIM11 protein is composed of three domains: an N-terminal domain that contains a nucleotide-binding oligomerization domain (NBO), a middle domain that contains a conserved nucleotide-binding oligomerization domain (NBO), and an C-terminal domain that contains a GFP-encoded protein. The NBO and NBO domains are responsible for the protein's nuclear localization and the ability to interact with DNA-binding proteins, while the GFP-encoded protein provides the protein with a fluorescent tag for visualization in live cells.

TRIM11 is a transmembrane protein, which means that it spans the cell membrane and is involved in the regulation of various cellular processes that are critical for cell survival. One of the most important functions of TRIM11 is its role in cell division. In eukaryotic cells, TRIM11 is involved in the regulation of mitosis, meiosis, and the G1/G2 phase of the cell cycle. During mitosis, TRIM11 is essential for the proper formation of the nuclear envelope and the development of accurate chromosome behavior during the cell division process. Similarly , during meiosis, TRIM11 is involved in the regulation of homologous recombination, which is a critical process for the formation of genetic diversity in the cell.

TRIM11 has also been shown to play a role in the regulation of apoptosis, which is a critical process for the elimination of damaged or dysfunctional cells. During apoptosis, TRIM11 is involved in the formation of a quality control system for cell death, which includes the production of apoptosis-associated proteins (APPs) such as caspases and ethylene-associated proteins. These APPs play a crucial role in the execution of cell death and are involved in the regulation of various cellular processes that are necessary for cell survival.

In addition to its role in cell division and apoptosis, TRIM11 has also been shown to be involved in the regulation of inflammation and immune responses. It is a known regulator of the NF-kappa-B signaling pathway, which is involved in the regulation of inflammation and immune responses. immune responses. TRIM11 has also been shown to play a role in the regulation of cell adhesion and migration, which are critical processes for the recruitment of immune cells to sites of infection or inflammation.

TRIM11 has also been identified as a potential drug target in the treatment of various diseases. For example, TRIM11 has been shown to be involved in the regulation of the development and progression of cancer, and is therefore a potential target for cancer therapies. Additionally, TRIM11 has been shown to be involved in the regulation of neurodegenerative diseases, and is therefore a potential target for neurodegenerative therapies.

In conclusion, TRIM11 is a protein that is involved in the regulation of various cellular processes that are critical for cell survival. Its role in cell division, apoptosis, inflammation, and immune responses makes it a potential drug target for the treatment of various diseases. Further research is needed to fully understand the mechanisms of TRIM11's function and its potential as a drug target.

Protein Name: Tripartite Motif Containing 11

Functions: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX (By similarity). Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis (By similarity). May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences (By similarity). May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway (By similarity). Mediates MED15 ubiquitination leading to proteasomal degradation (PubMed:16904669). May contribute to the innate restriction of retroviruses (PubMed:18248090). Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression (PubMed:18248090). Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain (PubMed:18248090). May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle (PubMed:18248090). Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2 (PubMed:27498865). Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (PubMed:27498865)

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•   general information;
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•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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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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