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Retinoid X receptor alpha (RXRα) interaction with sugars
Author(s) -
Soman Frances L,
Jesus Piva Camila,
Hostetler Heather A.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1012.3
Subject(s) - retinoid x receptor , liver x receptor , peroxisome proliferator activated receptor , nuclear receptor , biochemistry , chemistry , receptor , alpha (finance) , microbiology and biotechnology , biology , transcription factor , gene , medicine , construct validity , nursing , patient satisfaction
Nuclear receptors, peroxisome proliferator‐activated receptor alpha (PPARα) and liver X receptor alpha (LXRα), with their heterodimeric partner, RXRα, regulate transcriptional activity of lipid and glucose metabolism. It has been shown that glucose binds with high affinity to PPARα, and that transcriptional activity induced by the PPARα‐RXRα heterodimer increases in the presence of glucose. LXRα has also been shown to bind glucose, resulting in altered activity. As heterodimerization with RXRα is required for activation, we examined the ability of RXRα to interact with glucose and other sugars using fluorescent ligand binding assays and circular dichroism. While preliminary data with a GST‐tagged human RXRα protein suggested strong interactions with sugars, recent data with a tag‐free protein demonstrates significant conformational differences between these proteins. Although glucose did not significantly alter RXRα secondary structure, some sugars and sweeteners did. Such interactions may affect RXRα's role in heterodimerization and gene regulation. This research was supported by USPHS NIH grant DK77573.