GR Utilizes a Co-Chaperone Cytoplasmic CAR Retention Protein to Form an N/C Interaction.

ABSTRACT: The N-terminal domain (NTD) of nuclear receptor superfamily members has been recently reported to regulate functions of the receptor through the interaction between the NTD and the C-terminal ligand binding domain (LBD), so-called an N/C interaction. Although this N/C interaction has been demonstrated in various nuclear receptors, eg, androgen receptor, this concept has not been observed in glucocorticoid receptor (GR). We hypothesized that GR requires its co-chaperone CCRP (cytoplasmic constitutive active/androstane receptor retention protein) to form a stable N/C interaction. This hypothesis was examined by co-immunoprecipitation assays using GR fragments overexpressing COS-1 cell lysate. Here, we demonstrated that GR undergoes the N/C interaction between the ²⁶VMDFY³⁰

SUBMITTER: Ohno M 

PROVIDER: S-EPMC6348740 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature