OASL

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

59 kDa 2'-5'-oligoadenylate synthetase-like protein is an enzyme that in humans is encoded by the OASL gene.[5][6]

PDBOrtholog search: PDBe RCSB
AliasesOASL, OASLd, TRIP-14, TRIP14, p59 p59-p592'-5'-oligoadenylate synthetase like, OASL1
Quick facts Available structures, PDB ...
OASL
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesOASL, OASLd, TRIP-14, TRIP14, p59 p59-p592'-5'-oligoadenylate synthetase like, OASL1
External IDsOMIM: 603281; MGI: 2180849; HomoloGene: 2769; GeneCards: OASL; OMA:OASL - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_198213
NM_001261825
NM_003733
NM_001395418
NM_001395419

NM_145209
NM_001359945
NM_001359946

RefSeq (protein)

NP_001248754
NP_003724
NP_937856

NP_660210
NP_001346874
NP_001346875

Location (UCSC)Chr 12: 121.02 – 121.04 MbChr 5: 115.06 – 115.08 Mb
PubMed search[3][4]
Wikidata
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2'-5'-oligoadenylate synthase is a protein family of structurally similar proteins, including OAS1, OAS2, and OAS3. However, mutations in the OAS domain mean it lacks the motif to allow oligomerization, preventing the synthesis of oligoadenylates. OASL, like the proteins of 2'-5'-oligoadenylate synthase family, is induced by interferons.

Function

RNA Virus Infection

In RNA virus infection, viral genetic material binds to the RNA sensor RIG-I, triggering a reaction cascade that culminates in the secretion of type I interferons.[7] OASL acts as a sensitiser of RIG-I, binding to the caspase activation and recruitment domain and enhancing interferon production.[8]

DNA Virus Infection

While OASL has an anti-viral role in RNA viral infection, it has also demonstrated a pro-viral role in DNA viral infection.[9] OASL can bind to the viral DNA sensor cGAS, inhibiting its catalytic activity and preventing the secretion of interferons.[10]

Intracellular Bacterial Infection

OASL is shown to be upregulated during a wide variety of vacuolar and cytosolic bacterial infections.[11] It possesses an ability to inhibit autophagic mechanisms and antimicrobial peptide secretion within the host cell through unclear mechanisms, preventing clearance of the pathogen and creating a favourable intracellular environment.[12]

See also


References

Further reading

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