ARIH1: for Ubiquitin-Proteasome Complex Involvement in Neurological Disorders

Target Name: ARIH1

NCBI ID: G25820

ARIH1

ARIH1: for Ubiquitin-Proteasome Complex Involvement in Neurological Disorders

ARIH1: A Potential Drug Target and Biomarker for Ubiquitin-Proteasome Complex (UPC) Involvement in Neurological Disorders

The ubiquitin-proteasome (UPC) system is a complex protein network that plays a crucial role in protein homeostasis, cell signaling, and disease development. Disruptions in the UPC can lead to a wide range of neurological disorders, including neurodegenerative diseases, developmental disorders, and autoimmune disorders. The ARIH1 protein is a key player in the UPC and has been implicated in the development and progression of several neurological disorders. In this article, we will discuss the ARIH1 protein, its functions in the UPC, and its potential as a drug target and biomarker for neurological disorders.

The UPC and its Components

The UPC is a complex protein network that consists of multiple subunits that interact with each other to perform various functions in protein homeostasis and cell signaling. The UPC plays a critical role in the delivery, processing, and degradation of proteins, as well as the regulation of gene expression and cell signaling. The UPC is composed of several subunits, including the 尾2 subunit, the 纬 subunit, the 蔚 subunit, the 味 subunit, and the 畏 subunit.

The ARIH1 Protein

The ARIH1 protein is a member of the NED-RING family of ubiquitin ligases, which are involved in the regulation of protein-protein interactions and the formation of protein-nucleus bonds. The ARIH1 protein was identified as a potential drug target and biomarker for neurological disorders due to its involvement in the UPC and its ability to modulate the activity of the UPC.

The ARIH1 Protein Functions in the UPC

The ARIH1 protein functions as a ligase that adds a ubiquitin tag to target proteins. The ubiquitin tag is a short segment of amino acids that consists of 20-30 amino acids and is attached to the target protein via a disulfide bond. The ARIH1 protein uses a specific specificity parameter, known as \" specificity constant,\" to regulate the addition of the ubiquitin tag to the target protein. The specificity constant is a measure of the ability of the ARIH1 protein to recognize and bind to a specific protein.

The ARIH1 Protein in neurological disorders

The ARIH1 protein is involved in the regulation of several neurological disorders, including Alzheimer's disease, Parkinson's disease, and Huntington's disease. These disorders are characterized by the progressive loss of brain cells and the development of neurodegeneration. The ARIH1 protein has been shown to play a role in the development and progression of these disorders by modulating the activity of the UPC.

ARIH1 has been shown to increase the activity of the UPC and enhance the formation of protein-protein bonds. This increase in UPC activity has been linked to the development of neurodegeneration in individuals with Alzheimer's disease and Parkinson's disease. Additionally, the ARIH1 protein has been shown to reduce the clearance of toxic protein aggregates, which are thought to contribute to the neurodegeneration in these disorders.

The ARIH1 Protein as a Biomarker

The ARIH1 protein has also been shown to be a potential biomarker for neurological disorders. The ARIH1 protein has been shown to be expressed in the brains of individuals with Alzheimer's disease and Parkinson's disease, and its levels have been correlated with the severity of the disorders. Additionally, the ARIH1 protein has been shown to be a potential target for small molecule inhibitors, which could be used

Protein Name: Ariadne RBR E3 Ubiquitin Protein Ligase 1

Functions: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592, PubMed:24076655, PubMed:27565346, PubMed:23707686). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets (PubMed:27565346). The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 (PubMed:27565346). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes (PubMed:24076655, PubMed:27565346). Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear (PubMed:25624349). According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report EIF4E2 ubiquitination leads to its subsequent degradation (PubMed:14623119). Acts as the ligase involved in ISGylation of EIF4E2 (PubMed:17289916). In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology (PubMed:29689197)

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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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