ArticleNature communications2016
Super-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmenti.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- NEMO/IKKγ: Emerging player in the NF-κB pathway and potential therapeutic target in inflammation.Inflammation · 2026Review
- Review
- HDX-MS Analysis of Catalytic Activation of IKK2 in the IκB Kinase Complex.Biochemistry · 2024Article
- Molecular mechanism of IKK catalytic dimer docking to NF-κB substrates.Nature communications · 2024Article
- Secondary interactions in ubiquitin-binding domains achieve linkage or substrate specificity.Cell reports · 2024Article
- A conserved core region of the scaffold NEMO is essential for signal-induced conformational change and liquid-liquid phase separation.The Journal of biological chemistry · 2023Article
- A Conserved Core Region of the Scaffold NEMO is Essential for Signal-induced Conformational Change and Liquid-liquid Phase Separation.bioRxiv : the preprint server for biology · 2023Article
- Linear ubiquitination induces NEMO phase separation to activate NF-κB signaling.Life science alliance · 2023Article
- IκB kinase β (IKKβ): Structure, transduction mechanism, biological function, and discovery of its inhibitors.International journal of biological sciences · 2023Review
- Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.Nature communications · 2022Article
- Review
- Mechanistic insights into the activation of the IKK kinase complex by the Kaposi's sarcoma herpes virus oncoprotein vFLIP.The Journal of biological chemistry · 2022Article
- Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.bioRxiv : the preprint server for biology · 2021Article
- A self-exciting point process to study multicellular spatial signaling patterns.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A variable-gain stochastic pooling motif mediates information transfer from receptor assemblies into NF-κB.Science advances · 2021Article
- Article
- Targeting IKKβ in Cancer: Challenges and Opportunities for the Therapeutic Utilisation of IKKβ Inhibitors.Cells · 2018Review
- CCBuilder 2.0: Powerful and accessible coiled-coil modeling.Protein science : a publication of the Protein Society · 2018Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
The NF-κB pathway has critical roles in cancer, immunity and inflammatory responses. Understanding the mechanism(s) by which mutations in genes involved in the pathway cause disease has provided valuable insight into its regulation, yet many aspects remain unexplained. Several lines of evidence have led to the hypothesis that the regulatory/sensor protein NEMO acts as a biological binary switch. This hypothesis depends on the formation of a higher-order structure, which has yet to be identified using traditional molecular techniques. Here we use super-resolution microscopy to reveal the existence of higher-order NEMO lattice structures dependent on the presence of polyubiquitin chains before NF-κB activation. Such structures may permit proximity-based trans-autophosphorylation, leading to cooperative activation of the signalling cascade. We further show that NF-κB activation results in modification of these structures. Finally, we demonstrate that these structures are abrogated in cells derived from incontinentia pigmenti patients.
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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.