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TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures
Nuclear factor κB (NF-κB) essential modulator (NEMO), a regulatory component of the IκB kinase (IKK) complex, controls NF-κB activation through its interaction with ubiquitin chains. We show here that stimulation with interleukin-1 (IL-1) and TNF induces a rapid and transient recruitment of NEMO int...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897181/ https://www.ncbi.nlm.nih.gov/pubmed/24446482 http://dx.doi.org/10.1083/jcb.201307172 |
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author | Tarantino, Nadine Tinevez, Jean-Yves Crowell, Elizabeth Faris Boisson, Bertrand Henriques, Ricardo Mhlanga, Musa Agou, Fabrice Israël, Alain Laplantine, Emmanuel |
author_facet | Tarantino, Nadine Tinevez, Jean-Yves Crowell, Elizabeth Faris Boisson, Bertrand Henriques, Ricardo Mhlanga, Musa Agou, Fabrice Israël, Alain Laplantine, Emmanuel |
author_sort | Tarantino, Nadine |
collection | PubMed |
description | Nuclear factor κB (NF-κB) essential modulator (NEMO), a regulatory component of the IκB kinase (IKK) complex, controls NF-κB activation through its interaction with ubiquitin chains. We show here that stimulation with interleukin-1 (IL-1) and TNF induces a rapid and transient recruitment of NEMO into punctate structures that are anchored at the cell periphery. These structures are enriched in activated IKK kinases and ubiquitinated NEMO molecules, which suggests that they serve as organizing centers for the activation of NF-κB. These NEMO-containing structures colocalize with activated TNF receptors but not with activated IL-1 receptors. We investigated the involvement of nondegradative ubiquitination in the formation of these structures, using cells deficient in K63 ubiquitin chains or linear ubiquitin chain assembly complex (LUBAC)-mediated linear ubiquitination. Our results indicate that, unlike TNF, IL-1 requires K63-linked and linear ubiquitin chains to recruit NEMO into higher-order complexes. Thus, different mechanisms are involved in the recruitment of NEMO into supramolecular complexes, which appear to be essential for NF-κB activation. |
format | Online Article Text |
id | pubmed-3897181 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38971812014-07-20 TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures Tarantino, Nadine Tinevez, Jean-Yves Crowell, Elizabeth Faris Boisson, Bertrand Henriques, Ricardo Mhlanga, Musa Agou, Fabrice Israël, Alain Laplantine, Emmanuel J Cell Biol Research Articles Nuclear factor κB (NF-κB) essential modulator (NEMO), a regulatory component of the IκB kinase (IKK) complex, controls NF-κB activation through its interaction with ubiquitin chains. We show here that stimulation with interleukin-1 (IL-1) and TNF induces a rapid and transient recruitment of NEMO into punctate structures that are anchored at the cell periphery. These structures are enriched in activated IKK kinases and ubiquitinated NEMO molecules, which suggests that they serve as organizing centers for the activation of NF-κB. These NEMO-containing structures colocalize with activated TNF receptors but not with activated IL-1 receptors. We investigated the involvement of nondegradative ubiquitination in the formation of these structures, using cells deficient in K63 ubiquitin chains or linear ubiquitin chain assembly complex (LUBAC)-mediated linear ubiquitination. Our results indicate that, unlike TNF, IL-1 requires K63-linked and linear ubiquitin chains to recruit NEMO into higher-order complexes. Thus, different mechanisms are involved in the recruitment of NEMO into supramolecular complexes, which appear to be essential for NF-κB activation. The Rockefeller University Press 2014-01-20 /pmc/articles/PMC3897181/ /pubmed/24446482 http://dx.doi.org/10.1083/jcb.201307172 Text en © 2014 Tarantino et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Tarantino, Nadine Tinevez, Jean-Yves Crowell, Elizabeth Faris Boisson, Bertrand Henriques, Ricardo Mhlanga, Musa Agou, Fabrice Israël, Alain Laplantine, Emmanuel TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures |
title | TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures |
title_full | TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures |
title_fullStr | TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures |
title_full_unstemmed | TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures |
title_short | TNF and IL-1 exhibit distinct ubiquitin requirements for inducing NEMO–IKK supramolecular structures |
title_sort | tnf and il-1 exhibit distinct ubiquitin requirements for inducing nemo–ikk supramolecular structures |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897181/ https://www.ncbi.nlm.nih.gov/pubmed/24446482 http://dx.doi.org/10.1083/jcb.201307172 |
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