ArticleNature communications2018
Structural basis of RIP2 activation and signaling.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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Who cites it
47 citing papers in PubMed, 104 citations in OpenAlex.
- Structural insights into human caspase-9 CARD assembly modes driven by conserved arginine hotspots.Journal of structural biology: X · 2026Article
- Structural insights into ligand-induced CARD assembly in inflammatory caspases.Research square · 2026Article
- Multiple organ dysfunction syndrome: molecular mechanisms and therapeutic strategies.Signal transduction and targeted therapy · 2026Review
- Uncovering the Targets of Pueraria Associated with Programmed Cell Death and the Construction of a Diagnostic Model in Septic Cardiomyopathy.Biomedicines · 2026Article
- Structural and dynamic basis of NOD2 tandem CARD association and NOD1/2-RIP2 signaling complexes.PLoS computational biology · 2026Article
- Article
- Pattern recognition receptor signaling in otitis media: immune crosstalk and pathogenic mechanisms.Frontiers in immunology · 2026Review
- Distinct colitis-associated macrophages drive NOD2-dependent bacterial sensing and gut homeostasis.The Journal of clinical investigation · 2025Article
- A derivative of tanshinone IIA and salviadione, 15a, inhibits inflammation and alleviates DSS-induced colitis in mice by direct binding and inhibition of RIPK2.Acta pharmacologica Sinica · 2025Article
- Apaf-1 is an evolutionarily conserved DNA sensor that switches the cell fate between apoptosis and inflammation.Cell discovery · 2025Article
- MYSM1 attenuates osteoarthritis by recruiting PP2A to deubiquitinate and dephosphorylate RIPK2.Bone research · 2025Article
- Autophagy and Bacterial infections.Autophagy reports · 2025Review
- Current advances on RIPK2 and its inhibitors in pathological processes: a comprehensive review.Frontiers in molecular neuroscience · 2025Review
- Nucleotide-binding oligomerization domain 1 (NOD1) regulates microglial activation in pseudorabies virus infection.Veterinary research · 2024Article
- NOD1 and NOD2: Essential Monitoring Partners in the Innate Immune System.Current issues in molecular biology · 2024Review
- The Role of Pyroptosis and Autophagy in the Nervous System.Molecular neurobiology · 2024Review
- Innate Immune Response to Monkeypox Virus Infection: Mechanisms and Immune Escape.Journal of innate immunity · 2024Review
- NOD2 attenuates osteoarthritis via reprogramming the activation of synovial macrophages.Arthritis research & therapy · 2023Article
- A Bacterial Quorum Sensing Regulated Protease Inhibits Host Immune Responses by Cleaving Death Domains of Innate Immune Adaptors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- iE-DAP Induced Inflammatory Response and Tight Junction Disruption in Bovine Mammary Epithelial Cells via NOD1-Dependent NF-κB and MLCK Signaling Pathway.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Signals arising from bacterial infections are detected by pathogen recognition receptors (PRRs) and are transduced by specialized adapter proteins in mammalian cells. The Receptor-interacting-serine/threonine-protein kinase 2 (RIPK2 or RIP2) is such an adapter protein that is critical for signal propagation of the Nucleotide-binding-oligomerization-domain-containing proteins 1/2 (NOD1 and NOD2). Dysregulation of this signaling pathway leads to defects in bacterial detection and in some cases autoimmune diseases. Here, we show that the Caspase-activation-and-recruitment-domain (CARD) of RIP2 (RIP2-CARD) forms oligomeric structures upon stimulation by either NOD1-CARD or NOD2-2CARD. We reconstitute this complex, termed the RIPosome in vitro and solve the cryo-EM filament structure of the active RIP2-CARD complex at 4.1 Å resolution. The structure suggests potential mechanisms by which CARD domains from NOD1 and NOD2 initiate the oligomerization process of RIP2-CARD. Together with structure guided mutagenesis experiments at the CARD-CARD interfaces, we demonstrate molecular mechanisms how RIP2 is activated and self-propagating such signal.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.