Unknown

Dataset Information

0

Glucocorticoid Receptor-mediated transactivation is hampered by Striatin-3, a novel interaction partner of the receptor.


ABSTRACT: The transcriptional activity of the glucocorticoid receptor (GR) is co-determined by its ability to recruit a vast and varying number of cofactors. We here identify Striatin-3 (STRN3) as a novel interaction partner of GR that interferes with GR's ligand-dependent transactivation capacity. Remarkably, STRN3 selectively affects only GR-dependent transactivation and leaves GR-dependent transrepression mechanisms unhampered. We found that STRN3 down-regulates GR transactivation by an additional recruitment of the catalytic subunit of protein phosphatase 2A (PPP2CA) to GR. We hypothesize the existence of a functional trimeric complex in the nucleus, able to dephosphorylate GR at serine 211, a known marker for GR transactivation in a target gene-dependent manner. The presence of STRN3 appears an absolute prerequisite for PPP2CA to engage in a complex with GR. Herein, the C-terminal domain of GR is essential, reflecting ligand-dependency, yet other receptor parts are also needed to create additional contacts with STRN3.

SUBMITTER: Petta I 

PROVIDER: S-EPMC5567040 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Glucocorticoid Receptor-mediated transactivation is hampered by Striatin-3, a novel interaction partner of the receptor.

Petta Ioanna I   Bougarne Nadia N   Vandewalle Jolien J   Dejager Lien L   Vandevyver Sofie S   Ballegeer Marlies M   Desmet Sofie S   Thommis Jonathan J   De Cauwer Lode L   Lievens Sam S   Libert Claude C   Tavernier Jan J   De Bosscher Karolien K  

Scientific reports 20170821 1


The transcriptional activity of the glucocorticoid receptor (GR) is co-determined by its ability to recruit a vast and varying number of cofactors. We here identify Striatin-3 (STRN3) as a novel interaction partner of GR that interferes with GR's ligand-dependent transactivation capacity. Remarkably, STRN3 selectively affects only GR-dependent transactivation and leaves GR-dependent transrepression mechanisms unhampered. We found that STRN3 down-regulates GR transactivation by an additional recr  ...[more]

Similar Datasets

| S-EPMC5614576 | biostudies-literature
| S-EPMC2678648 | biostudies-literature
| S-EPMC6890434 | biostudies-literature
| S-EPMC5419154 | biostudies-literature
| S-EPMC8325269 | biostudies-literature
| S-EPMC1356362 | biostudies-literature
| S-EPMC3904736 | biostudies-literature
| S-EPMC3039389 | biostudies-literature
| S-EPMC5461336 | biostudies-literature
| S-EPMC5431531 | biostudies-literature