Gilardi F Desvergne B 2014 Retinoid X Receptors (RXR) were initially identified as nuclear receptors binding with stereo-selectivity the vitamin A derivative 9-cis retinoic acid, although the relevance of this molecule as endogenous activator of RXRs is still elusive. Importantly, within the nuclear receptor superfamily, RXRs occupy a peculiar place, as they are obligatory partners for a number of other nuclear receptors, thus integrating the corresponding signaling pathways. In this chapter, we describe the structural features allowing RXR to form homo- and heterodimers, and the functional consequences of this unique ability. Furthermore, we discuss the importance of studying RXR activity at a genome-wide level in order to comprehensively address the biological implications of their action that is fundamental to understand to what extent RXRs could be exploited as new therapeutic targets. https://sonar.ch/global/documents/246288 eng info:eu-repo/semantics/altIdentifier/doi/10.1007/978-94-017-9050-5_5 info:eu-repo/semantics/altIdentifier/pmid/24962882 Sub-cellular biochemistry. - 2014 Alitretinoin Animals Gene Expression Regulation Humans Ligands Mice Protein Binding Protein Isoforms Protein Multimerization Protein Structure, Tertiary Receptors, Retinoic Acid Response Elements Retinoid X Receptors Signal Transduction Tretinoin RXRs: collegial partners. http://purl.org/coar/resource_type/c_6501