ART-27, an Androgen Receptor Coactivator Regulated in Prostate Development and Cancer

Taneja, Samir S.; Ha, Susan; Swenson, Nicole; Pineda-Torra, Inés; Rome, Serge; Walden, Paul D.; Huang, Hong; Shapiro, Ellen; Garabedian, Michael J.; Logan, Susan K.

doi:10.1074/jbc.m306576200

Cited by 57 publications

(47 citation statements)

References 43 publications

(39 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In vivo staining showed that URI, Art-27, and AR were expressed in prostate epithelial cells (Fig. 5d), with only negligible URI and Art-27 expression in the stroma, as previously reported (23). These observations indicate that AR, URI, and the AR cofactor Art-27 are colocalized in prostate epithelial cells.…”

Section: Uri Represses Ar-mediated Gene Transcription It Has Beensupporting

confidence: 65%

Regulation of Androgen Receptor-Mediated Transcription by RPB5 Binding Protein URI/RMP

Mita

Savas

Djouder

et al. 2011

Molecular and Cellular Biology

Self Cite

View full text Add to dashboard Cite

Androgen receptor (AR)-mediated transcription is modulated by interaction with coregulatory proteins. We demonstrate that the unconventional prefoldin RPB5 interactor (URI) is a new regulator of AR transcription and is critical for antagonist (bicalutamide) action. URI is phosphorylated upon androgen treatment, suggesting communication between the URI and AR signaling pathways. Whereas depletion of URI enhances AR-mediated gene transcription, overexpression of URI suppresses AR transcriptional activation and anchorage-independent prostate cancer cell growth. Repression of AR-mediated transcription is achieved, in part, by URI binding and regulation of androgen receptor trapped clone 27 (Art-27), a previously characterized AR corepressor. Consistent with this idea, genome-wide expression profiling in prostate cancer cells upon depletion of URI or Art-27 reveals substantially overlapping patterns of gene expression. Further, depletion of URI increases the expression of the AR target gene NKX-3.1, decreases the recruitment of Art-27, and increases AR occupancy at the NKX-3.1 promoter. While Art-27 can bind AR directly, URI is bound to chromatin prior to hormone-dependent recruitment of AR, suggesting a role for URI in modulating AR recruitment to target genes.

show abstract

Section: Uri Represses Ar-mediated Gene Transcription It Has Beensupporting

confidence: 65%

Regulation of Androgen Receptor-Mediated Transcription by RPB5 Binding Protein URI/RMP

Mita

Savas

Djouder

et al. 2011

Molecular and Cellular Biology

Self Cite

View full text Add to dashboard Cite

show abstract

“…This once considered "ubiquitously expressed transcript" is actually tightly regulated both in a cell line-and developmental stage-specific fashion and is downregulated in prostate cancer cells, consistent with a role as an inhibitor of androgen-mediated cellular proliferation (Taneja et al 2004;Nwachukwu et al 2007). In a separate study, UXT was also shown to bind the transcriptional repressor Evi1 and inhibit its cell transformation property in Rat1 cells (McGilvray et al 2007).…”

Section: Uxt (Art-27/stap1)mentioning

confidence: 76%

New insights into the biogenesis of nuclear RNA polymerases?This paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Cloutier

Coulombe

2010

Biochem. Cell Biol.

View full text Add to dashboard Cite

More than 30 years of research on nuclear RNA polymerases (RNAP I, II, and III) has uncovered numerous factors that regulate the activity of these enzymes during the transcription reaction. However, very little is known about the machinery that regulates the fate of RNAPs before or after transcription. In particular, the mechanisms of biogenesis of the 3 nuclear RNAPs, which comprise both common and specific subunits, remains mostly uncharacterized and the proteins involved are yet to be discovered. Using protein affinity purification coupled to mass spectrometry (AP-MS), we recently unraveled a high-density interaction network formed by nuclear RNAP subunits from the soluble fraction of human cell extracts. Validation of the dataset using a machine learning approach trained to minimize the rate of false positives and false negatives yielded a highconfidence dataset and uncovered novel interactors that regulate the RNAP II transcription machinery, including a set of proteins we named the RNAP II-associated proteins (RPAPs). One of the RPAPs, RPAP3, is part of an 11-subunit complex we termed the RPAP3/R2TP/prefoldin-like complex. Here, we review the literature on the subunits of this complex, which points to a role in nuclear RNAP biogenesis.

show abstract

“…Consistent with these results, proliferation of LNCaP cells and colony formation were inhibited after overexpression of ARA70, thus suggesting its role as a tumour suppressor. There is also evidence that expression levels of the coactivator AR trapped clone-27 (ART-27) are substantially decreased in prostate cancer tissues (Taneja et al 2004).…”

Section: Ar Coactivator Alterations Occur In Endocrine Therapy-resistmentioning

confidence: 99%

Mechanisms of endocrine therapy-responsive and -unresponsive prostate tumours

Čulig¹,

Steiner²,

Bartsch³

et al. 2005

Endocrine-Related Cancer

View full text Add to dashboard Cite

Several options for the endocrine treatment of non-organ-confined prostate cancer are available. They include surgical or medical removal of androgenic hormones or administration of non-steroidal anti-androgens. However, tumour progression after a period of remission of the disease inevitably occurs in virtually all patients. The androgen receptor (AR) is, in various tumour models, implicated in the development of therapy resistance but molecular mechanisms that by-pass the receptor have also been described. Adaptation mechanisms relevant to tumour recurrence include up-regulation of AR mRNA and protein, overexpression of AR coactivators, increased activation of mutated receptors by steroids and anti-androgens, and ligand-independent activation. For research studies, sublines that respond to but do not depend on androgen for their proliferation were generated. Coactivators SRC-1, TIF-2, RAC3, p300, CBP, Tip60, and gelsolin are highly expressed in endocrine therapy-resistant prostate cancer. AR point mutations are increasingly detected in relapsed cancers and contribute to the failure of endocrine therapy in a subgroup of patients. Ligand-independent activation of the AR by HER-2/neu and interleukin-6 is associated with activation of the signalling pathway of mitogen-activated protein kinase. Increased activity of intracellular kinases may affect cellular events in both an AR-dependent and -independent manner. Mitogen-activated protein kinases are strongly phosphorylated in endocrine therapy-resistant prostate tumours. Similarly, activation of the AR by phosphorylated protein kinase B, Akt, has also been reported in prostate cancer. Activation of the Akt pathway contributes to increased survival of prostate tumour cells.

show abstract

ART-27, an Androgen Receptor Coactivator Regulated in Prostate Development and Cancer

Cited by 57 publications

References 43 publications

Regulation of Androgen Receptor-Mediated Transcription by RPB5 Binding Protein URI/RMP

Regulation of Androgen Receptor-Mediated Transcription by RPB5 Binding Protein URI/RMP

Mechanisms of endocrine therapy-responsive and -unresponsive prostate tumours

Contact Info

Product

Resources

About