Diversity of Quaternary Structures Regulates Nuclear Receptor Activities

Pablo Fuentes-Prior; Ana Rojas; Arnold T Hagler; Eva Estébanez-Perpiñá

doi:10.1016/j.tibs.2018.09.005

Diversity of Quaternary Structures Regulates Nuclear Receptor Activities

Trends Biochem Sci. 2019 Jan;44(1):2-6. doi: 10.1016/j.tibs.2018.09.005. Epub 2018 Oct 4.

Authors

Pablo Fuentes-Prior¹, Ana Rojas², Arnold T Hagler³, Eva Estébanez-Perpiñá⁴

Affiliations

¹ Molecular Bases of Disease, Biomedical Research Institute Sant Pau (IIB Sant Pau), 08025 Barcelona, Spain; Equally contributing authors. Electronic address: pfuentes@santpau.cat.
² Computational Biology and Bioinformatics, Andalusian Center for Developmental Biology (CABD-CSIC), 41013 Seville, Spain.
³ Department of Chemistry, University of Massachusetts, Amherst, MA, USA.
⁴ Department of Biochemistry and Molecular Biomedicine, Institute of Biomedicine (IBUB), University of Barcelona (UB), 08028 Barcelona, Spain; Equally contributing authors. Electronic address: evaestebanez@ub.edu.

PMID: 30293659
DOI: 10.1016/j.tibs.2018.09.005

Abstract

Nuclear receptors (NRs) form homo- and/or heterodimers as central scaffolds of multiprotein complexes, which activate or repress gene transcription to regulate development, homeostasis, and metabolism. Recent studies on NR quaternary structure reveal novel mechanisms of receptor dimerization, the existence of tetrameric chromatin-bound NRs, and previously unanticipated protein-protein/protein-DNA interactions.

Keywords: Nuclear receptors; monomer-oligomer transition; protein–protein interaction surfaces; quaternary structure; structure–function.

MeSH terms

Binding Sites
DNA / chemistry
DNA / metabolism
Humans
Models, Molecular
Protein Binding
Protein Structure, Quaternary
Receptors, Cytoplasmic and Nuclear / chemistry*
Receptors, Cytoplasmic and Nuclear / genetics
Receptors, Cytoplasmic and Nuclear / metabolism*

Substances

Receptors, Cytoplasmic and Nuclear
DNA