The RIG-I System: A conservative Innate Immune Response Receptor and Potential Drug Target

Target Name: RIGI

NCBI ID: G23586

RIGI

The RIG-I System: A conservative Innate Immune Response Receptor and Potential Drug Target

The RIGI (RIG-I) system is a critical innate immune response receptor that plays a crucial role in the regulation of immune responses and inflammation. RIG-I is a member of the cytoplasmic adaptor family, which includes proteins that interact with intracellular signaling molecules to regulate various cellular processes. The RIG-I system is highly conserved across different species, and its involvement in the innate immune response has been extensively studied in the past decade.

The RIG-I system is involved in the regulation of several key cellular processes, including the perception of pathogens, inflammation, and cellular stress. RIG-I is expressed in many different cell types, including epithelial cells, macrophages, dendritic cells, and hematopoietic cells. It is involved in the regulation of various cellular signaling pathways, including the TLR (Toll-like receptor) signaling pathway, which is involved in the recognition of pathogens by the immune system.

One of the well-established functions of RIG-I is its role in the regulation of the cytokine network. Cytokines are small signaling molecules that are produced by various cell types in response to different stimuli, including pathogens and cellular stress. These molecules play a crucial role in the regulation of cellular processes, including inflammation, cell adhesion, and survival. The RIG-I system is involved in the regulation of the cytokine network by several mechanisms, including the inhibition of the JAK/STAT signaling pathway, which is involved in the regulation of cytokine signaling.

Another function of RIG-I is its role in the regulation of cellular stress. cellular stress refers to the damage caused to cellular components that can result from various cellular processes, including oxidative stress, DNA damage, and inflammation. RIG-I is involved in the regulation of cellular stress by several mechanisms, including the inhibition of the DNA damage-associated kinase (DACA) pathway, which is involved in the regulation of DNA damage repair.

RIG-I is also involved in the regulation of inflammation. Inflammation is a critical immune response to pathogens, and it is associated with various cellular processes, including the production of pro-inflammatory cytokines and the recruitment of immune cells to the site of inflammation. The RIG-I system is involved in the regulation of inflammation by several mechanisms, including the inhibition of the NF-kappa-B signaling pathway, which is involved in the regulation of inflammation.

In addition to its role in the regulation of cellular processes, RIG-I is also a potential drug target. The RIG-I system has been extensively studied in the past decade, and several studies have identified potential drug targets associated with RIG-I. For example, several studies have identified potential inhibitors of RIG-I that are currently being developed as potential therapeutic agents for various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

Overall, the RIG-I system is a critical innate immune response receptor that plays a crucial role in the regulation of cellular processes, including the perception of pathogens, inflammation, and cellular stress. Its involvement in these processes makes it an attractive target for the development of new therapeutic agents for various diseases. The continued study of the RIG-I system and its potential drug targets has the potential to lead to new treatments for a variety of diseases.

Protein Name: RNA Sensor RIG-I

Functions: Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines (PubMed:15208624, PubMed:16125763, PubMed:15708988, PubMed:16127453, PubMed:16153868, PubMed:17190814, PubMed:18636086, PubMed:19122199, PubMed:19211564, PubMed:29117565, PubMed:28469175, PubMed:31006531, PubMed:34935440, PubMed:35263596). Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments (PubMed:15208624, PubMed:15708988). The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms (PubMed:28469175, PubMed:31006531). Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons (PubMed:28469175, PubMed:31006531). Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length) (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV) (PubMed:21616437, PubMed:21884169). It also detects rotaviruses and reoviruses (PubMed:21616437, PubMed:21884169). Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.67). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV) (PubMed:19631370). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration

The "RIGI 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 RIGI 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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