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Zoglowek, A., Orlowski, M., Pakula, S., Dutko-Gwozdz, J., Pajdzik, D., Gwozdz, T., Rymarczyk, G., Wieczorek, E., Dobrucki, J., Dobryszycki, P., Ozyhar, A. (2012). The composite nature of the interaction between nuclear receptors EcR and DHR38.  Biol. Chem. 393(6): 457--471.
FlyBase ID
FBrf0218420
Publication Type
Research paper
Abstract
Ecdysteroids coordinate essential biological processes in Drosophila through a complex of two nuclear receptors, the ecdysteroid receptor (EcR) and the ultraspiracle protein (Usp). Biochemical experiments have shown that, in contrast to Usp, the EcR molecule is characterized by high intramolecular plasticity. To investigate whether this plasticity is sufficient to form EcR complexes with nuclear receptors other than Usp, we studied the interaction of EcR with the DHR38 nuclear receptor. Previous in vitro experiments suggested that DHR38 can form complexes with Usp and thus disrupt Usp-EcR interaction with the specific hsp27pal response element. This article provides the experimental evidence that EcR is able to form complexes with DHR38 as well. The recombinant DNA-binding domains (DBDs) of EcR and DHR38 interact specifically on hsp27pal. However, the interaction between the receptors is not restricted to their isolated DBDs. We present data that indicate that the full-length EcR and DHR38 can also form specific complexes within the nuclei of living cells. This interaction is mediated by the hinge region of EcR, which was recently classified as an intrinsically disordered region. Our results indicate that DHR38 might modulate the activity of the Usp-EcR heterodimer by forming complexes with both of its components.
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Biol. Chem.
    Title
    Biological chemistry
    Publication Year
    1996-
    ISBN/ISSN
    1431-6730
    Data From Reference
    Genes (4)
    Physical Interactions (2)