ArticleScientific reports2016
Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 47 citations in OpenAlex.
- Identification of small-molecule inhibitors of the immune system repressor Regnase-1.NAR molecular medicine · 2026Article
- Article
- The Regnase pathway: a core axis in immune regulation and inflammatory disease.Frontiers in immunology · 2026Review
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- MCPIP1 Elicits a Therapeutic Effect on Cervical Cancer by Facilitating XIAP mRNA Decay via Its Endoribonuclease Activity.International journal of molecular sciences · 2024Article
- Crosstalk between Regnase-1 and -3 shapes mast cell survival and cytokine expression.Life science alliance · 2024Article
- N4BP1 functions as a dimerization-dependent linear ubiquitin reader which regulates TNF signalling.Cell death discovery · 2024Article
- Crystallization and biochemical studies of the NYN domain of human KHNYN.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Lung Epithelial Regnase-1 Dampens Local Immune Response but Does Not Worsen Susceptibility to Klebsiella pneumoniae.ImmunoHorizons · 2024Article
- UPF1-From mRNA Degradation to Human Disorders.Cells · 2023Review
- ZC3H12C expression in dendritic cells is necessary to prevent lymphadenopathy of skin-draining lymph nodes.Immunology and cell biology · 2022Article
- Article
- IRAK1-dependent Regnase-1-14-3-3 complex formation controls Regnase-1-mediated mRNA decay.eLife · 2021Article
- Extracellular mRNA transported to the nucleus exerts translation-independent function.Nature communications · 2021Article
- PIN and CCCH Zn-finger domains coordinate RNA targeting in ZC3H12 family endoribonucleases.Nucleic acids research · 2021Article
- Monocyte chemoattractant protein-induced protein 1 directly degrades viral miRNAs with a specific motif and inhibits KSHV infection.Nucleic acids research · 2021Article
- Roquin is a major mediator of iron-regulated changes to transferrin receptor-1 mRNA stability.iScience · 2021Article
- Conceptual Advances in Control of Inflammation by the RNA-Binding Protein Tristetraprolin.Frontiers in immunology · 2021Review
- Analysis of Protein Intermolecular Interactions with MAFFT-DASH.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Monocyte Chemotactic Protein-Induced Protein 1 (MCPIP-1): A Key Player of Host Defense and Immune Regulation.Frontiers in immunology · 2021Review
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regnase-1 is an RNase that directly cleaves mRNAs of inflammatory genes such as IL-6 and IL-12p40, and negatively regulates cellular inflammatory responses. Here, we report the structures of four domains of Regnase-1 from Mus musculus-the N-terminal domain (NTD), PilT N-terminus like (PIN) domain, zinc finger (ZF) domain and C-terminal domain (CTD). The PIN domain harbors the RNase catalytic center; however, it is insufficient for enzymatic activity. We found that the NTD associates with the PIN domain and significantly enhances its RNase activity. The PIN domain forms a head-to-tail oligomer and the dimer interface overlaps with the NTD binding site. Interestingly, mutations blocking PIN oligomerization had no RNase activity, indicating that both oligomerization and NTD binding are crucial for RNase activity in vitro. These results suggest that Regnase-1 RNase activity is tightly controlled by both intramolecular (NTD-PIN) and intermolecular (PIN-PIN) interactions.
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