Origin of the Functional Distinctiveness of NF-κB/p52.

Gourisankar Ghosh,Vivien Ya-Fan Wang

doi:10.3389/fcell.2021.764164

Gourisankar Ghosh, Vivien Ya-Fan Wang

Open Access

https://doi.org/10.3389/fcell.2021.764164

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Abstract

The transcription regulators of the NF-κB family have emerged as a critical factor affecting the function of various adult tissues. The NF-κB family transcription factors are homo- and heterodimers made up of five monomers (p50, p52, RelA, cRel and RelB). The family is distinguished by sequence homology in their DNA binding and dimerization domains, which enables them to bind similar DNA response elements and participate in similar biological programs through transcriptional activation and repression of hundreds of genes. Even though the family members are closely related in terms of sequence and function, they all display distinct activities. In this review, we discuss the sequence characteristics, protein and DNA interactions, and pathogenic involvement of one member of family, NF-κB/p52, relative to that of other members. We pinpoint the small sequence variations within the conserved region that are mostly responsible for its distinct functional properties.

Highlights

Reviewed by: Soumen Basak, National Institute of Immunology (NII), India Neil Perkins, Newcastle University, United Kingdom
The family is distinguished by sequence homology in their DNA binding and dimerization domains, which enables them to bind similar DNA response elements and participate in similar biological programs through transcriptional activation and repression of hundreds of genes
The five NF-κB proteins can be further divided into two sub-classes: the p50 and p52 subunits belong to class I by virtue of their lack of a transcriptional activation domain (TAD)

Summary

Introduction

The family is distinguished by sequence homology in their DNA binding and dimerization domains, which enables them to bind similar DNA response elements and participate in similar biological programs through transcriptional activation and repression of hundreds of genes. This roughly 300 residues long segment is responsible for site-specific DNA binding, combinatorial dimer formation and inhibitor of NF-κB (IκB) protein binding.

Results

Conclusion