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      Regulation of androgen receptor transcriptional activity and specificity by RNF6-induced ubiquitination.

      Cancer Cell
      Amino Acid Sequence, Androgens, pharmacology, Animals, COS Cells, Cells, Cultured, Cercopithecus aethiops, Chromatin Immunoprecipitation, DNA-Binding Proteins, genetics, metabolism, Fluorescent Antibody Technique, Gene Expression Profiling, Humans, Immunoenzyme Techniques, Kidney, cytology, Male, Molecular Sequence Data, Neoplasms, Hormone-Dependent, Prostatic Hyperplasia, Prostatic Neoplasms, pathology, RNA, Messenger, Receptors, Androgen, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Transcription, Genetic, Ubiquitination

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          Abstract

          The androgen receptor (AR) plays a critical role in prostate cancer. We have identified a ubiquitin E3 ligase, RNF6, as an AR-associated protein in a proteomic screen. RNF6 induces AR ubiquitination and promotes AR transcriptional activity. Specific knockdown of RNF6 or mutation of RNF6-induced ubiquitination acceptor sites on AR selectively alters expression of a subset of AR target genes and diminishes recruitment of AR and its coactivators to androgen-responsive elements present in the regulatory region of these genes. Furthermore, RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Our data suggest that RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity through modulating cofactor recruitment.

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