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The Rel/NF-κB signal transduction pathway: introduction

Oncogene volume 18, pages 6842–6844 (1999)Cite this article

The Rel/NF-κB proteins are related through a highly conserved DNA-binding/dimerization domain called the Rel homology (RH) domain. However, they can be divided into two classes based on sequences Cterminal to the RH domain. Members of one class (p105, p100, and Drosophila Relish) have long C-terminal domains that contain multiple copies of ankyrin repeats, which act to inhibit these molecules. Members of this class become active, shorter DNA-binding proteins (p105 to p50, p100 to p52) by either limited proteolysis or arrested translation. As such, members of this first class are generally not activators of transcription, except when they form dimers with members of the second class of Rel/NF-κB transcription factors. The second class includes c-Rel (and its homologue v-Rel), RelB, RelA (p65), Dorsal, and Dif. These Rel proteins contain C-terminal activation domains, which are often not conserved at the sequence level across species, even though they can activate transcription in a variety of species.

Rel/NF-κB transcription factors bind to 10 base pair DNA sites (κB sites) as dimers. All vertebrate Rel proteins can form homodimers or heterodimers, except for RelB, which can only form heterodimers. This combinatorial diversity contributes to the regulation of distinct, but overlapping, sets of genes, in that the individual dimers have distinct DNA-binding site specificities for a collection of related κB sites. NF-κB commonly refers to a p50-RelA heterodimer, which is one of the most avidly forming dimers and is the major Rel complex in most cells.

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Acknowledgements

Foremost, I thank the authors for their timely contributions to this review issue. Collectively, we apologize to any researchers who feel that their work was overlooked in this collection. I thank C Li and members of my laboratory for critical reading of this article, and I thank the National Institutes of Health and the Council for Tobacco Research for their continued support of research in my laboratory on Rel/NF-κB signaling and oncogenesis.

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  1. Biology Department, Boston University, 5 Cummington Street, Boston, 02215-2406, Massachusetts, MA, USA

    Thomas D Gilmore

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Gilmore, T. The Rel/NF-κB signal transduction pathway: introduction. Oncogene 18, 6842–6844 (1999). https://doi.org/10.1038/sj.onc.1203237

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