期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 278, 期 17, 页码 14956-14960出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M212229200
关键词
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资金
- NCI NIH HHS [CA16672] Funding Source: Medline
The androgen receptor (AR) is a ligand-regulated and sequence-specific transcription factor that activates or represses expression of target genes. Here, we show that the N terminus of AR contains an inhibitory domain located in an 81-amino acid segment lying upstream of the DNA-binding domain (DBD). The inhibitory domain interacted directly with DBD and repressed DBD binding to the androgen response element. Mutations of the conserved amino acid residues (K520E and R538E) within the inhibitory domain decreased its inhibiting ability in vitro and increased AR trans-activation in vivo. These data demonstrate the existence of a novel inhibitory domain in the N-terminal part of AR, which might play important roles in the regulation of AR trans-activation.
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