Abstract
Cell death-inducing DNA fragmentation factor alpha-like effector A (CIDEA) is endogenously expressed in human but not rodent white adipocytes. We performed a bioinformatic analysis of the human CIDEA sequence and found conserved amino-acid motifs involved in binding to nuclear receptors. Protein–protein binding experiments and transactivation assays confirmed that CIDEA binds to liver X receptors and regulates their activity in vitro. Cell fractionation demonstrated that CIDEA localizes to both the cytoplasm and the nucleus in human white adipocytes. The interaction between CIDEA and nuclear receptors could therefore be of importance for the regulation of metabolic processes in human adipose tissue. Structured summary LXR-beta binds to CIDEA by pull down (View interaction) TIF2 and LXR-beta physically interact by two hybrid (View interaction) LXR-beta binds to RAP250 by pull down (View interaction) CIDEA and LXR-beta physically interact by two hybrid (View interaction)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
