1. Nuclear factor κB mutations in human subjects: The devil is in the details 
Manfred Fliegauf, PhD, Bodo Grimbacher, MD 
Journal of Allergy and Clinical Immunology 
Volume 142, Issue 4, Pages (October 2018)
DOI: /j.jaci
Copyright © 2018 American Academy of Allergy, Asthma & Immunology Terms and Conditions

2. Fig 1
The basic principle of canonical NF-κB signaling. Processing of the C-terminal half converts the NF-κB1 precursor p105 into mature p50, which assembles with RelA (also known as p65), a heteromeric transcriptional activator. The inhibitory protein IκBα is associated with cytoplasmic p50/RelA dimers. On pathway stimulation, activation of the trimeric upstream IκB kinase complex (IKK) leads to phosphorylation, polyubiquitination, and degradation of IκBα. Subsequently, p50/RelA is released from its inhibitor, translocates to the nucleus, and activates its target genes. Homodimers of p50 act as transcriptional repressors (not shown). BCR, B-cell receptor; RANK, receptor activator of NF-κB; TCR, T-cell receptor; TLR, Toll-like receptor.
Journal of Allergy and Clinical Immunology  , DOI: ( /j.jaci )
Copyright © 2018 American Academy of Allergy, Asthma & Immunology Terms and Conditions

3. Fig 2
NFKB1 mutations cluster into at least 4 groups. The schematic protein structure of the p105 precursor with the N-terminal Rel homology domain (RHD), the central nuclear localization sequence (NLS) and the glycine-rich region (GRR), and the C-terminal Ankyrin repeat domain (ANK) and the death domain (DD) is shown. Mature p50 comprises the N-terminal half of p105. Numbers indicate amino acid positions. Depending on the type and localization of a given mutation (indicated by horizontal black bars), miscellaneous protein functions and/or diverse signaling processes might be involved. Because of the complexity of NF-κB signaling, this concept is not exhaustive.
Journal of Allergy and Clinical Immunology  , DOI: ( /j.jaci )
Copyright © 2018 American Academy of Allergy, Asthma & Immunology Terms and Conditions