ADARB1: A Potential Drug Target and Biomarker for RNA-Specific Enrichment and Deamination

Target Name: ADARB1

NCBI ID: G104

ADARB1: A Potential Drug Target and Biomarker for RNA-Specific Enrichment and Deamination

Abstract:

ADARB1, or Adenosine deaminase, RNA-specific, B1 (RED1 homolog), is a gene that encodes a protein involved in the removal of adenosine, a nucleoside that plays a crucial role in various cellular processes, including signaling, inflammation, and stress responses. The RNA-specific nature of ADARB1's function and its unique localization to the endoplasmic reticulum (ER) have made it an attractive candidate for potential drug targets and biomarkers. In this article, we will explore the ADARB1 gene, its function, and its potential as a drug target and biomarker.

Introduction:

Adenosine, a nucleoside that contains a nitrogenous base and a phosphate group, is widely recognized for its role in various cellular processes. In addition to its role in signaling and inflammation, adenosine has also been linked to stress responses, neurotransmitter release, and memory. Its removal is critical for maintaining the homeostasis of the cell.

ADARB1, a gene encoding a protein involved in the removal of adenosine, has been identified as a potential drug target and biomarker. ADARB1's unique localization to the ER and its RNA-specific nature make it an attractive candidate for drug targeting.

Molecular Characterization:

The ADARB1 gene encodes a protein with a molecular weight of approximately 11 kDa. The protein has a single known function: to remove adenosine from various cellular compartments, including the ER. Adenosine removal is critical for maintaining the homeostasis of the cell, and the dysfunction in this process has been linked to various diseases, including neurodegenerative diseases, cancer, and cardiovascular diseases.

ADARB1 is expressed in various tissues and cells, including the brain, heart, and peripheral tissues. Its expression is highly dependent on the presence of adenosine, which is synthesized from other nucleosides, such as guanosine and uridine. Therefore, the levels of ADARB1 expression are regulated by the levels of these nucleosides.

Expression and localization:

ADARB1 is predominantly expressed in the ER, where it is involved in the removal of adenosine. The ER is a specialized organelle responsible for the synthesis and storage of proteins, and its structures are highly conserved across various species. The ER has a well-defined transmembrane system and a highly organized cytoskeleton, which are features that support the localization of ADARB1 to the ER.

The localization of ADARB1 to the ER is regulated by its interactivity with various factors, including adapter proteins and intracellular signaling pathways. For example, the protein Nrf2 has been shown to interact with ADARB1 and play a role in its localization to the ER. Nrf2 is a gene that encodes a protein involved in the detoxification of environmental toxins, and it has been implicated in various diseases, including neurodegenerative diseases.

Drug targeting:

ADARB1's unique localization to the ER and its RNA-specific nature make it an attractive candidate for drug targeting. Drugs that can specifically target the ER and enhance the localization of ADARB1 may have potential therapeutic applications in various diseases.

One approach to drug targeting is to use small molecules that can specifically interact with ADARB1 and enhance its localization to the ER. Compounds that have been shown to interact with ADARB1 include rapamycin, a drug used to prevent the negative effects of cellular

Protein Name: Adenosine Deaminase RNA Specific B1

Functions: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR while the latter occurs via suppression of EIF2AK2/PKR activation and function. Can inhibit cell proliferation and migration and can stimulate exocytosis

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