ArticleCell cycle (Georgetown, Tex.)2012
Androgen receptor serine 81 mediates Pin1 interaction and activity.
Article in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Pin1-catalyzed conformational regulation after phosphorylation: A distinct checkpoint in cell signaling and drug discovery.Science signaling · 2024Review
- New PIN1 inhibitors identified through a pharmacophore-driven, hierarchical consensus docking strategy.Journal of enzyme inhibition and medicinal chemistry · 2022Article
- Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis.Theranostics · 2021Review
- Posttranslational regulation of androgen dependent and independent androgen receptor activities in prostate cancer.Asian journal of urology · 2020Review
- Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics.Frontiers in cell and developmental biology · 2020Review
- Oncogenic Hijacking of the PIN1 Signaling Network.Frontiers in oncology · 2019Review
- Editorial: Peptidyl-Prolyl Isomerases in Human Pathologies.Frontiers in pharmacology · 2019Article
- Phosphorylation of androgen receptor serine 81 is associated with its reactivation in castration-resistant prostate cancer.Cancer letters · 2018Article
- A Guide to PIN1 Function and Mutations Across Cancers.Frontiers in pharmacology · 2018Article
- Article
- The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target.Nature reviews. Cancer · 2016Review
- Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α.The Journal of biological chemistry · 2015Article
- Article
- The prolyl isomerase pin1 regulates mRNA levels of genes with short half-lives by targeting specific RNA binding proteins.PloS one · 2014Article
- Proline-Directed Androgen Receptor Phosphorylation.Journal of molecular and genetic medicine : an international journal of biomedical research · 2013Article
- Pin1 promotes GR transactivation by enhancing recruitment to target genes.Nucleic acids research · 2013Article
- Phosphorylation: a fundamental regulator of steroid receptor action.Trends in endocrinology and metabolism: TEM · 2013Review
- Posttranslational modification of the androgen receptor in prostate cancer.International journal of molecular sciences · 2013Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hormone-dependent tumors are characterized by deregulated activity of specific steroid receptors, allowing aberrant expression of many genes involved in cancer initiation, progression and metastasis. In prostate cancer, the androgen receptor (AR) protein has pivotal functions, and over the years it has been the target of different drugs. AR is a nuclear receptor whose activity is regulated by a phosphorylation mechanism controlled by hormone and growth factors. Following phosphorylation, AR interacts with many cofactors that closely control its function. Among such cofactors, Pin1 is a peptidyl-prolyl isomerase that is involved in the control of protein phosphorylation and has a prognostic value in prostate cancer. In the present study, we demonstrate that ARSer81 is involved in the interaction with Pin1, and that this interaction is important for the transcriptional activity of AR. Since Pin1 expression positively correlates with tumor grade, our results suggest that Pin1 can participate in this process by modulating AR function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.