Identification of a Novel Coregulator, SH3YL1, That Interacts With the Androgen Receptor N-Terminus.

ABSTRACT: Nuclear receptor (NR)-mediated transcriptional activity is a dynamic process that is regulated by the binding of ligands that induce distinct conformational changes in the NR. These structural alterations lead to the differential recruitment of coregulators (coactivators or corepressors) that control the expression of NR-regulated genes. Here, we show that a stretch of proline residues located within the N-terminus of androgen receptor (AR) is a bona fide coregulator binding surface, the disruption of which reduces the androgen-dependent proliferation and migration of prostate cancer (PCa) cells. Using T7 phage display, we identified a novel AR-interacting protein, Src homology 3 (SH3)-domain containing, Ysc84-like 1 (SH3YL1), whose interaction with the receptor is dependent upon this poly

SUBMITTER: Blessing AM 

PROVIDER: S-EPMC4588732 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature