Identification of UFL1 as A Potential Drug Target for Neurodegenerative Diseases

Target Name: UFL1

NCBI ID: G23376

UFL1

Identification of UFL1 as A Potential Drug Target for Neurodegenerative Diseases

The UFL1 gene, located on chromosome 1p36.1, has been identified as a potential drug target and biomarker for the treatment of various neurological disorders, including Alzheimer's disease. UFL1 is a non-coding RNA molecule that is regulated by the transcription factor C53 and LZAP, as well as the microRNA DDRGK1.

The C53 transcription factor is a key regulator of gene expression in the brain, and is known to play a role in the development and progression of neurodegenerative diseases. The LZAP protein, which is also known as TCF7, is a negative regulator of the C53 transcription factor and has been implicated in the pathogenesis of various neurological disorders, including Alzheimer's disease.

The DDRGK1 microRNA is known for its role in the regulation of gene expression in the brain, and has been shown to be involved in the development and progression of neurodegenerative diseases.

The UFL1 gene has been shown to be regulated by the C53 and LZAP transcription factors, as well as DDRGK1. This suggests that UFL1 may play a role in the regulation of gene expression and the development and progression of neurodegenerative diseases.

In addition to its potential role as a drug target and biomarker, UFL1 also has potential as a therapeutic approach in the treatment of neurodegenerative diseases. The development of RNA-based therapeutics, such as UFL1-targeted drugs, may provide a new and effective way to treat these disorders.

In conclusion, the UFL1 gene has shown promising potential as a drug target and biomarker for the treatment of neurodegenerative diseases. Further research is needed to fully understand its role and to develop effective therapies based on this protein.

Protein Name: UFM1 Specific Ligase 1

Functions: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress (PubMed:20018847, PubMed:20164180, PubMed:20228063, PubMed:25219498, PubMed:32160526). In response to endoplasmic reticulum stress, recruited to the endoplasmic reticulum membrane by DDRGK1, and mediates ufmylation of proteins such as RPN1 and RPL26/uL24, thereby promoting reticulophagy of endoplasmic reticulum sheets (PubMed:32160526). Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) via ERN1/IRE1-alpha (PubMed:23152784, PubMed:32160526). Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response (PubMed:32050156). Regulates inflammation in response to endoplasmic reticulum stress by promoting reticulophagy, leading to inhibit the activity of the NF-kappa-B transcription factor (By similarity). Mediates ufmylation of DDRGK1 and CDK5RAP3; the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation (PubMed:20531390, PubMed:20018847). Catalyzes ufmylation of various subunits of the ribosomal complex or associated components, such as RPS3/uS3, RPS20/uS10, RPL10/uL16, RPL26/uL24 and EIF6 (By similarity). Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition (PubMed:20531390). Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 (PubMed:30886146). Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (PubMed:25219498). Required for hematopoietic stem cell function and hematopoiesis (By similarity). Required for cardiac homeostasis (By similarity)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   pharmacochemistry experiments;
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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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