Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12629
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Funding
- Department of Science and Technology of South Africa
- Young Researcher Establishment Fund, CSIR [YREF 2015 009]
- National Research Foundation Professional Development Programme Fund (NRF PDP)
- Fundacao para a Ciencia e a Tecnologia (FCT, Portugal) [PTDC/SAU-GMG/115652/2009]
- UK Medical Research Council [MR/K015826/1]
- UK Biotechnology and Biological Sciences Research Council [BB/M022374/1]
- Institut Pasteur:Citech
- Global care initiative
- Institut Carnot Pasteur MI
- BBSRC [BB/M022374/1] Funding Source: UKRI
- MRC [MR/K015826/1] Funding Source: UKRI
- Fundação para a Ciência e a Tecnologia [PTDC/SAU-GMG/115652/2009] Funding Source: FCT
- Biotechnology and Biological Sciences Research Council [BB/M022374/1] Funding Source: researchfish
- Medical Research Council [MR/K015826/1] Funding Source: researchfish
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The NF-kappa B 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-kappa B activation. Such structures may permit proximity-based trans-autophosphorylation, leading to cooperative activation of the signalling cascade. We further show that NF-kappa B 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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