Ring finger and CCCH-type domains 1 (RC3H1)

Ring finger and CCCH-type domains 1 (RC3H1), commonly known as Roquin-1, is a multifunctional RNA-binding protein and E3 ubiquitin ligase. It contains a RING finger domain (characteristic of E3 ubiquitin ligases), a ROQ domain, and a CCCH-type zinc finger domain, which allow it to recognize specific secondary RNA structures—mainly constitutive decay elements (CDEs)—in the 3′ untranslated regions (UTRs) of target mRNAs. RC3H1 mediates mRNA decay by recruiting deadenylase and decapping complexes (notably the CCR4-NOT complex), thus regulating post-transcriptional gene expression, particularly in immune-related transcripts like ICOS, OX40, A20, and TNFα. It thereby acts as a central regulator of immune homeostasis, inflammation, and T cell function. Mutations in RC3H1 are linked to severe immune dysregulation, including autoimmunity and hyperinflammatory syndromes. The protein is essential for limiting inappropriate T follicular helper cell activation and modulating signaling pathways such as NF-κB and the cellular DNA damage response[1][2][3][4][5][6][7].

Other names

Roquin-1KIAA2025RNF198RoquinRING finger and C3H zinc finger protein 1RING finger and CCCH-type zinc finger domain-containing protein 1RING finger protein 198FHL6IMDSHYprobable E3 ubiquitin-protein ligase RoquinRC3H1

Not applicable (no direct drugs, but theoretical mechanisms could involve inhibition or modulation of RNA/protein binding, E3 ligase activity, or enhancing/decreasing mRNA decay)