Multiple Signal Input and Output Domains of the 160-Kilodalton Nuclear Receptor Coactivator Proteins

• DOI: 10.1128/mcb.19.9.6164
• Publication Date: 2015-10-26T10:20:01Z
• Authors: Han Ma; Heng Hong; Shih-Ming Huang; Ryan A. Irvine; Paul Webb; Peter J. Kushner; Gerhard A. Coetzee; Michael R. Stallcup
• Keywords: CREB-binding protein

Members of the 160-kDa nuclear receptor coactivator family (p160 coactivators) bind to conserved AF-2 activation function found in hormone binding domains receptors (NR) and are potent transcriptional coactivators for NRs. Here we report that C-terminal region p160 glucocorticoid interacting protein 1 (GRIP1), steroid (SRC-1a), SRC-1e binds N-terminal AF-1 androgen (AR), can thereby enhance by AR. While they all interact efficiently with AR AF-1, these same have vastly different strengths effects on AF-2. domain AD1, which secondary CREB (CBP) p300, was previously implicated as principal transmitting activating signal transcription machinery. We identified a new highly motif AD1 is important CBP/p300 binding. Deletion only partially reduced function, due signaling through AD2, another located at end coactivators. fragments lacking but containing AD2 site served efficient full-length AF-1. The two input (one NR one some not NRs) output (AD1 AD2) played relative roles NRs: thyroid receptor.