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10.1038/ncomms12629 http://scihub22266oqcxt.onion/10.1038/ncomms12629 C5025789!5025789 !27586688     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27586688 &cmd=llinks): Failed to open stream: HTTP request failed! 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Super-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmenti |pdf=|usr=}}{{27586688 }} gab.com Text Super-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmenti JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27586688 #FOAvip The NF-?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-?B activation. Such structures may permit proximity-based trans-autophosphorylation, leading to cooperative activation of the signalling cascade. We further show that NF-?B activation results in modification of these structures. Finally, we demonstrate that these structures are abrogated in cells derived from incontinentia pigmenti patients. Twit Text FOAVip Super-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmenti ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27586688 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27586688 #FOAvip English Wikipedia <ref>{{Cite pmid|27586688 }}</ref> Super-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmenti #MMPMID27586688 Scholefield J ; Henriques R ; Savulescu AF ; Fontan E ; Boucharlat A ; Laplantine E ; Smahi A ; Israël A ; Agou F ; Mhlanga MM Nat Commun 2016[Sep]; 7 (ä): 12629 PMID27586688 show ga The NF-?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-?B activation. Such structures may permit proximity-based trans-autophosphorylation, leading to cooperative activation of the signalling cascade. We further show that NF-?B activation results in modification of these structures. Finally, we demonstrate that these structures are abrogated in cells derived from incontinentia pigmenti patients. |Cell Line, Tumor [MESH] |Enzyme Activation [MESH] |Humans [MESH] |I-kappa B Kinase/metabolism/physiology/*ultrastructure [MESH] |Incontinentia Pigmenti/*pathology [MESH] |Microscopy/*methods [MESH] |NF-kappa B/*metabolism [MESH] |Protein Binding [MESH] |Protein Structure, Secondary [MESH]Super-resolution microscopy reveals a preformed NEMO lattice structure(epmc).pdf DeepDyve Pubget Overpricing