Cargando…

Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases

The study of antiviral pathways to reveal methods for the effective response and clearance of virus is closely related to understanding interferon (IFN) signaling and its downstream target genes, IFN-stimulated genes. One of the key antiviral factors induced by IFNs, 2′-5′ oligoadenylate synthase (O...

Descripción completa

Detalles Bibliográficos
Autores principales: Choi, Un Yung, Kang, Ji-Seon, Hwang, Yune Sahng, Kim, Young-Joon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4351405/
https://www.ncbi.nlm.nih.gov/pubmed/25744296
http://dx.doi.org/10.1038/emm.2014.110
_version_ 1782360317187063808
author Choi, Un Yung
Kang, Ji-Seon
Hwang, Yune Sahng
Kim, Young-Joon
author_facet Choi, Un Yung
Kang, Ji-Seon
Hwang, Yune Sahng
Kim, Young-Joon
author_sort Choi, Un Yung
collection PubMed
description The study of antiviral pathways to reveal methods for the effective response and clearance of virus is closely related to understanding interferon (IFN) signaling and its downstream target genes, IFN-stimulated genes. One of the key antiviral factors induced by IFNs, 2′-5′ oligoadenylate synthase (OAS), is a well-known molecule that regulates the early phase of viral infection by degrading viral RNA in combination with RNase L, resulting in the inhibition of viral replication. In this review, we describe OAS family proteins from a different point of view from that of previous reviews. We discuss not only RNase L-dependent (canonical) and -independent (noncanonical) pathways but also the possibility of the OAS family members as biomarkers for various diseases and clues to non-immunological functions based on recent studies. In particular, we focus on OASL, a member of the OAS family that is relatively less well understood than the other members. We will explain its anti- and pro-viral dual roles as well as the diseases related to single-nucleotide polymorphisms in the corresponding gene.
format Online
Article
Text
id pubmed-4351405
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-43514052015-03-10 Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases Choi, Un Yung Kang, Ji-Seon Hwang, Yune Sahng Kim, Young-Joon Exp Mol Med Review The study of antiviral pathways to reveal methods for the effective response and clearance of virus is closely related to understanding interferon (IFN) signaling and its downstream target genes, IFN-stimulated genes. One of the key antiviral factors induced by IFNs, 2′-5′ oligoadenylate synthase (OAS), is a well-known molecule that regulates the early phase of viral infection by degrading viral RNA in combination with RNase L, resulting in the inhibition of viral replication. In this review, we describe OAS family proteins from a different point of view from that of previous reviews. We discuss not only RNase L-dependent (canonical) and -independent (noncanonical) pathways but also the possibility of the OAS family members as biomarkers for various diseases and clues to non-immunological functions based on recent studies. In particular, we focus on OASL, a member of the OAS family that is relatively less well understood than the other members. We will explain its anti- and pro-viral dual roles as well as the diseases related to single-nucleotide polymorphisms in the corresponding gene. Nature Publishing Group 2015-03 2015-03-06 /pmc/articles/PMC4351405/ /pubmed/25744296 http://dx.doi.org/10.1038/emm.2014.110 Text en Copyright © 2014 KSBMB. http://creativecommons.org/licenses/by/3.0/ This work is licensed under a Creative Commons Attribution 3.0 Unported License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/
spellingShingle Review
Choi, Un Yung
Kang, Ji-Seon
Hwang, Yune Sahng
Kim, Young-Joon
Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
title Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
title_full Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
title_fullStr Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
title_full_unstemmed Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
title_short Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases
title_sort oligoadenylate synthase-like (oasl) proteins: dual functions and associations with diseases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4351405/
https://www.ncbi.nlm.nih.gov/pubmed/25744296
http://dx.doi.org/10.1038/emm.2014.110
work_keys_str_mv AT choiunyung oligoadenylatesynthaselikeoaslproteinsdualfunctionsandassociationswithdiseases
AT kangjiseon oligoadenylatesynthaselikeoaslproteinsdualfunctionsandassociationswithdiseases
AT hwangyunesahng oligoadenylatesynthaselikeoaslproteinsdualfunctionsandassociationswithdiseases
AT kimyoungjoon oligoadenylatesynthaselikeoaslproteinsdualfunctionsandassociationswithdiseases