2'-5'-oligoadenylate synthase-dependent ribonuclease L (RNase L) (RNase L)

2'-5'-oligoadenylate synthase-dependent ribonuclease L, commonly known as RNase L, is a critical endoribonuclease involved in the mammalian innate immune response against viral infections [1, 2]. It is part of the interferon-induced 2-5A system, where interferon signaling triggers the production of 2'-5'-oligoadenylates (2-5A) that bind to and activate RNase L [3]. Once activated, RNase L dimerizes and cleaves single-stranded RNA, effectively halting viral replication and inducing apoptosis in infected cells [4, 5]. Beyond its antiviral properties, RNase L acts as a tumor suppressor; mutations in the RNASEL gene are associated with hereditary prostate cancer (HPC1) [2, 3]. Therapeutic interest in RNase L focuses on developing small molecule activators to treat viral infections and certain cancers, although challenges remain regarding the specificity of RNA degradation and potential toxicity to healthy cells [1, 4].

Other names

Ribonuclease L2-5A-dependent ribonucleaseRNASELRNS4Ribonuclease 4HPC12'-5'-oligoadenylate synthetase-dependent ribonuclease L

Activation by 2'-5'-oligoadenylates (2-5A) leads to dimerization and subsequent cleavage of single-stranded viral and cellular RNA [1, 3].