CBL: Enzyme in The Regulation of Protein Degradation (G867)

Target Name: CBL

NCBI ID: G867

Content of Review Report on CBL Target / Biomarker

CBL

CBL: Enzyme in The Regulation of Protein Degradation

CBL ( Ubiquitin-Protein Ligase ) is an enzyme that plays a crucial role in the regulation of protein degradation in the cell. It is a part of the ubiquitin system, which is a network of proteins that help to break down and remove damaged or unnecessary proteins from the cell. CBL is an essential enzyme in this system, and its activity is regulated by a variety of factors.

One of the key functions of CBL is to recognize and bind to specific protein targets. These targets are ubiquitinated proteins, which means that they have a Ubiquitin molecule attached to them. Once CBL has bound to a target protein, it can then use its catalytic activity to remove the Ubiquitin molecule, effectively breaking down the target protein.

CBL is also involved in the regulation of protein stability. By breaking down Ubiquitin molecules, CBL helps to maintain the stability of the target proteins, which is important for their correct function and survival in the cell. Additionally, CBL can also play a role in the regulation of cellular signaling pathways, by participating in the degradation of signaling proteins that have become excessively phosphorylated.

CBL is also a potent drug target, and several studies have identified potential inhibitors that could be used to treat a variety of diseases. For example, CBL has been shown to be involved in the regulation of the development and progression of cancer, and inhibitors of CBL have been shown to have therapeutic effects against cancer cells. Additionally, CBL has also been shown to be involved in the regulation of autoimmune diseases, and inhibitors of CBL have been shown to have therapeutic effects in treating autoimmune diseases.

Another potential application of CBL as a drug target is its role in the treatment of neurodegenerative diseases. CBL has been shown to be involved in the regulation of the degradation of the protein tau, which is abnormally phosphorylated in several neurodegenerative diseases, including Alzheimer's disease .Therefore, inhibitors of CBL have been shown to have therapeutic effects in treating neurodegenerative diseases.

In addition to its potential therapeutic applications, CBL also has important structural and functional roles in several cellular processes. For example, CBL is a key component of the ubiquitin-protein ligase complex, which is responsible for the degradation of a wide variety of proteins. Additionally, CBL is also involved in the regulation of the assembly and disassembly of other proteins, such as the protein N-telomerase.

Overall, CBL is a complex enzyme that plays a crucial role in the regulation of protein degradation in the cell. Its activity is regulated by a variety of factors, including its interactions with protein targets, its role in the regulation of protein stability, and its involved in cellular signaling pathways. Additionally, CBL is a potent drug target, with several studies identifying potential inhibitors that could be used to treat a variety of diseases. As its role in the regulation of protein degradation continues to be understood, the potential applications of CBL as a drug target will continue to be explored.

Protein Name: Cbl Proto-oncogene

Functions: Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:17094949). Ubiquitinates SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates EGFR (PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity)

The "CBL 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 CBL 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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