ArticleJournal of immunology (Baltimore, Md. : 1950)2016
Synthetic Biology Reveals the Uniqueness of the RIP Kinase Domain.
Article in Journal of immunology (Baltimore, Md. : 1950), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Plasma genome-wide mendelian randomization identifies potentially causal genes in idiopathic pulmonary fibrosis.Respiratory research · 2024Article
- Expression of Truncated Products at the 5'-Terminal Region of RIPK2 and Evolutive Aspects that Support Their Biological Importance.Genome biology and evolution · 2024Article
- Exploring the prognostic significance of arm-level copy number alterations in triple-negative breast cancer.Oncogene · 2024Article
- Structure shows that the BIR2 domain of E3 ligase XIAP binds across the RIPK2 kinase dimer interface.Life science alliance · 2023Article
- Functions of the RIP kinase family members in the skin.Cellular and molecular life sciences : CMLS · 2023Review
- Virulence Factors ofPathogens (Basel, Switzerland) · 2023Review
- Protein engineering reveals that gasdermin A preferentially targets mitochondrial membranes over the plasma membrane during pyroptosis.The Journal of biological chemistry · 2023Article
- Article
- LncRNA LINC01537 Promotes Gastric Cancer Metastasis and Tumorigenesis by Stabilizing RIPK4 to Activate NF-κB Signaling.Cancers · 2022Article
- RIPK4 Is an Immune Regulating-Associated Biomarker for Ovarian Cancer and Possesses Generalization Value in Pan-Cancer.Journal of immunology research · 2022Article
- Human polymorphisms in GSDMD alter the inflammatory response.The Journal of biological chemistry · 2020Article
- Article
- Unique BIR domain sets determine inhibitor of apoptosis protein-driven cell death and NOD2 complex signal specificity.Science signaling · 2018Article
- Article
- Structures of the Gasdermin D C-Terminal Domains Reveal Mechanisms of Autoinhibition.Structure (London, England : 1993) · 2018Article
- Role of the NFκB-signaling pathway in cancer.OncoTargets and therapy · 2018Review
- Live-cell visualization of gasdermin D-driven pyroptotic cell death.The Journal of biological chemistry · 2017Article
- Nucleotide-binding oligomerization domain (NOD) signaling defects and cell death susceptibility cannot be uncoupled in X-linked inhibitor of apoptosis (XIAP)-driven inflammatory disease.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The RIP kinases (RIPKs) play an essential role in inflammatory signaling and inflammatory cell death. However, the function of their kinase activity has been enigmatic, and only recently has kinase domain activity been shown to be crucial for their signal transduction capacity. Despite this uncertainty, the RIPKs have been the subject of intense pharmaceutical development with a number of compounds currently in preclinical testing. In this work, we seek to determine the functional redundancy between the kinase domains of the four major RIPK family members. We find that although RIPK1, RIPK2, and RIPK4 are similar in that they can all activate NF-κB and induce NF-κB essential modulator ubiquitination, only RIPK2 is a dual-specificity kinase. Domain swapping experiments showed that the RIPK4 kinase domain could be converted to a dual-specificity kinase and is essentially indistinct from RIPK2 in biochemical and molecular activity. Surprisingly, however, replacement of RIPK2's kinase domain with RIPK4's did not complement a nucleotide-binding oligomerization domain 2 signaling or gene expression induction defect in RIPK2(-/-) macrophages. These findings suggest that RIPK2's kinase domain is functionally unique compared with other RIPK family members and that pharmacologic targeting of RIPK2 can be separated from the other RIPKs.
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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.