Author Name: Keith Howell

Category Name: Medical science

Description:

Nuclear Factor kappa-light-chain-enhancer of activated B cells or NF-κB  is found in almost all animal cells and is a protein complex that controls the transcription of DNA. This protein complex is involved in numerous cellular responses and plays a key role in regulating the immune response to infection. NF-κB is also implicated in processes of synaptic plasticity and memory that require additional avenues of research to flesh out completely the possibilities and uses of this compound.
All proteins of the NF-κB family share a Rel homology domain in their N-terminus. A subfamily of NF-κB proteins, including RelA, RelB, and c-Rel, have a transactivation domain in their C-termini. In contrast, the NF-κB1 and NF-κB2 proteins are synthesized as large precursors, undergoing processing to generate mature and active NF-κB subunits. 
NF-κB is detected in most cell types, and specific NF-κB binding sites are identified in promoters and enhancers of increasing number of inducible genes. The transcription factor NF-κB consists of homo- or heterodimers of different subunits, members of a family of structurally related proteins–Rel/NF-κB proteins. Rel proteins contain a conserved N-terminal region, called the Rel Homology Domain (RHD), which contains the DNA-binding and dimerization domains and the nuclear localization signal of the Rel proteins. NF-κB can be activated by a number of stimuli, including exposure of cells to Lipopolysaccharides or inflammatory cytokines such as Tumor Necrosis Factor or Interleukin-1, growth factors, lymphokines, oxidant-free radicals, inhaled particles, viral infection or expression of certain viral or bacterial gene products.  Activation of NF-κB occurs according to specific and sequential phosphorylation of residues such as Ser32 and Ser36 of IκBa leading to proteasome - mediated degradation. Further, phosphorylation of Ser 276 on RelA/p65 allows its oligomerization and reulation of DNA-binding. NF-κB phosphorylation is crucial for the regulation of the NF-κB Activation.

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Media Contact:

Kieth Howell
Journal Manager
Journal of Cell signaling
Email: cellsignaling@peerjournal.org