Hienosäätöä tulee RIG1:iin monista sinkkiproteiineista ja niitä säätelemällä taas inflammasomit vaikuttavat tähän RNA- helikaasiin, joka voisi tunnistaa soluun tulleen viruksen RNA:ta. Esim NLRP12 johtaa RIG-1 molekyyliä silppuriin ja NNLRC5 estää RIG-1- MAVS ineraktion.
- GeneCards Symbol: DDX58 2
- DExD/H-Box Helicase 58 2 3 5
- RIG-I 2 3 4 5
- RIG-1 2 4 5
- RIG1 2 3 5
- Antiviral Innate Immune Response Receptor RIG-I 3 4
- DEAD (Asp-Glu-Ala-Asp) Box Polypeptide 58 2 3
- Retinoic Acid-Inducible Gene 1 Protein 3 4
- Retinoic Acid-Inducible Gene I Protein 3 4
- ATP-Dependent RNA Helicase DDX58 3 4
- DEAD Box Protein 58 3 4
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DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. This gene encodes a protein containing RNA helicase-DEAD box protein motifs and a caspase recruitment domain (CARD). It is involved in viral double-stranded (ds) RNA recognition and the regulation of the antiviral innate immune response. Mutations in this gene are associated with Singleton-Merten syndrome 2. [provided by RefSeq, Aug 2020]
DDX58 (DExD/H-Box Helicase 58) is a Protein Coding gene. Diseases associated with DDX58 include Singleton-Merten Syndrome 2 and Singleton-Merten Syndrome. Among its related pathways are Metabolism of proteins and SARS-CoV-2 Infection. Gene Ontology (GO) annotations related to this gene include nucleic acid binding and hydrolase activity. An important paralog of this gene is ENSG00000288684.
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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). 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).(Kommentti RNF135 RING zinc finger-proteiini omaa muita nimiä:L13, MMFD, REUL, Riplet)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 (RSV) 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.65).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.
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