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

Janine Scholefield; Ricardo Henriques; Anca F. Savulescu; Elisabeth Fontan; Alix Boucharlat; Emmanuel Laplantine; Asma Smahi; Alain Israël; Fabrice Agou; Musa M. Mhlanga

doi:10.1038/ncomms12629

Nature Communications (Sep 2016)

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

Janine Scholefield,
Ricardo Henriques,
Anca F. Savulescu,
Elisabeth Fontan,
Alix Boucharlat,
Emmanuel Laplantine,
Asma Smahi,
Alain Israël,
Fabrice Agou,
Musa M. Mhlanga

Affiliations

Janine Scholefield: Division of Chemical Systems and Synthetic Biology, Faculty of Health Sciences, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Anzio Road, Observatory, Cape Town, Western Cape 7925, South Africa
Ricardo Henriques: MRC Laboratory for Molecular Cell Biology and Department of Cell and Developmental Biology, Quantitative Imaging and Nanobiophysics Group, University College London
Anca F. Savulescu: Division of Chemical Systems and Synthetic Biology, Faculty of Health Sciences, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Anzio Road, Observatory, Cape Town, Western Cape 7925, South Africa
Elisabeth Fontan: Departments of Cell Biology and Infection and of Structural Biology and Chemistry, Chemogenomic and Biological Screening Core Facility, Institut Pasteur, Center for Innovation and Technological Research (Citech)
Alix Boucharlat: Departments of Cell Biology and Infection and of Structural Biology and Chemistry, Chemogenomic and Biological Screening Core Facility, Institut Pasteur, Center for Innovation and Technological Research (Citech)
Emmanuel Laplantine: Laboratory of Signaling and Pathogenesis, CNRS, UMR 3691, Institut Pasteur
Asma Smahi: INSERM U1163-Université Paris Descartes-Sorbonne Paris Cité, Institut Imagine, Hôpital Necker-Enfants Malades
Alain Israël: Laboratory of Signaling and Pathogenesis, CNRS, UMR 3691, Institut Pasteur
Fabrice Agou: Departments of Cell Biology and Infection and of Structural Biology and Chemistry, Chemogenomic and Biological Screening Core Facility, Institut Pasteur, Center for Innovation and Technological Research (Citech)
Musa M. Mhlanga: Division of Chemical Systems and Synthetic Biology, Faculty of Health Sciences, Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Anzio Road, Observatory, Cape Town, Western Cape 7925, South Africa

DOI: https://doi.org/10.1038/ncomms12629
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 13

Abstract

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NEMO is a member of the IKK complex that binds ubiquitin, involved in NF-κB signalling and proposed to form higher order structures. Here the authors use super-resolution microscopy to detect the presence of NEMO lattices in cells, that are modified by NF-κB treatment and abrogated by mutations affecting NEMO ubiquitin binding.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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