The AF1 and AF2 Domains of the Androgen Receptor Interact with Distinct Regions of SRC1

AUTOR(ES)

Bevan, Charlotte L.

FONTE

American Society for Microbiology

RESUMO

The androgen receptor is unusual among nuclear receptors in that most, if not all, of its activity is mediated via the constitutive activation function in the N terminus. Here we demonstrate that p160 coactivators such as SRC1 (steroid receptor coactivator 1) interact directly with the N terminus in a ligand-independent manner via a conserved glutamine-rich region between residues 1053 and 1123. Although SRC1 is capable of interacting with the ligand-binding domain by means of LXXLL motifs, this interaction is not essential since an SRC1 mutant with no functional LXXLL motifs retains its ability to potentiate androgen receptor activity. In contrast, mutants lacking the glutamine-rich region are inactive, indicating that this region is both necessary and sufficient for recruitment of SRC1 to the androgen receptor. This recruitment is in direct contrast to the recruitment of SRC1 to the estrogen receptor, which requires interaction with the ligand-binding domain.

Documentos Relacionados

• Synergy between estrogen receptor α activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2
• TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain
• Analysis of the Steroid Receptor Coactivator 1 (SRC1)-CREB Binding Protein Interaction Interface and Its Importance for the Function of SRC1
• Two Domains of the Progesterone Receptor Interact with the Estrogen Receptor and Are Required for Progesterone Activation of the c-Src/Erk Pathway in Mammalian Cells
• Bioferramenta analítica : produção e desenvolvimento empregando anticorpo monoclonal antiaflatoxina (hibridoma AF2 e AF4)