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Super-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmenti

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dc.contributor.authorScholefield, Janine
dc.contributor.authorHenriques, Ricardo
dc.contributor.authorSavulescu, Anca F.
dc.contributor.authorFontan, Elisabeth
dc.contributor.authorBoucharlat, Alix
dc.contributor.authorLaplantine, Emmanuel
dc.contributor.authorSmahi, Asma
dc.contributor.authorIsraël, Alain
dc.contributor.authorAgou, Fabrice
dc.contributor.authorMhlanga, Musa
dc.date.accessioned2022-05-19T14:41:28Z
dc.date.available2022-05-19T14:41:28Z
dc.date.issued2016
dc.description© The Author(s) 2016.This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/pt_PT
dc.description.abstractThe 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.pt_PT
dc.description.sponsorshipThis work was funded by the Department of Science and Technology of South Africa. A.F.S. is funded by a Young Researcher Establishment Fund, CSIR (YREF 2015 009) and J.S. by the National Research Foundation Professional Development Programme Fund (NRF PDP). M.M.M. and R.H. are funded by PTDC/SAU-GMG/115652/2009 from the Fundação para a Ciência e a Tecnologia (FCT, Portugal). R.H. is funded by grants from the UK Medical Research Council (MR/K015826/1) and UK Biotechnology and Biological Sciences Research Council (BB/M022374/1). F.A. acknowledges funding from Institut Pasteur:Citech, Global care initiative and Institut Carnot Pasteur MI.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationNat Commun. 2016 Sep 2;7:12629pt_PT
dc.identifier.doi10.1038/ncomms12629pt_PT
dc.identifier.eissn2041-1723
dc.identifier.urihttp://hdl.handle.net/10451/53074
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherSpringer Naturept_PT
dc.relationSuper-resolution Imaging of Gene Expression & Nuclear Architecture
dc.relation.publisherversionhttps://www.nature.com/ncomms/pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleSuper-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmentipt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumberPTDC/SAU-GMG/115652/2009
oaire.awardTitleSuper-resolution Imaging of Gene Expression & Nuclear Architecture
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FSAU-GMG%2F115652%2F2009/PT
oaire.citation.issue1pt_PT
oaire.citation.titleNature Communicationspt_PT
oaire.citation.volume7pt_PT
oaire.fundingStream3599-PPCDT
person.familyNameMhlanga
person.givenNameMusa
person.identifier.orcid0000-0003-1381-3409
person.identifier.ridD-1283-2011
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication8aa5f7f2-ad5d-4274-b6f0-a9e3684795c3
relation.isAuthorOfPublication.latestForDiscovery8aa5f7f2-ad5d-4274-b6f0-a9e3684795c3
relation.isProjectOfPublication9c3edab3-4e39-41de-a000-8a0b5f3728dc
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