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

Un Yung Choi, Ji Seon Kang, Yune Sahng Hwang, Young Joon Kim

Research output: Contribution to journalReview articlepeer-review

136 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article numbere144
JournalExperimental and Molecular Medicine
Volume47
Issue number3
DOIs
Publication statusPublished - 2015

Bibliographical note

Funding Information:
This research was supported by the Global Research Laboratory Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST, K20705000006-12A0500-00610 to Y-JK), the Bio and Medical Technology Development Program of the National Research Foundation (NRF) funded by the Ministry of Science, ICT and Future Planning (MEST, 2012028272 to Y-JK) and the Korea Health Technology R&D Project through the Korea Health Industry Development Institute (KHIDI), funded by the Ministry of Health and Welfare, Republic of Korea (grant number: HI13C08470200).

Publisher Copyright:
© 2015 KSBMB. All rights reserved.

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry

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