ArticlePloS one2013
The prolyl isomerase Pin1 acts synergistically with CDK2 to regulate the basal activity of estrogen receptor α in breast cancer.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Circulating Pin1 Levels in Patients With Chronic Thromboembolic Pulmonary Hypertension: A Case-Control Study.Pulmonary circulation · 2025Article
- Temperature-sensitive sodium beta-glycerophosphate/chitosan hydrogel loaded with all-trans retinoic acid regulates Pin1 to inhibit the formation of spinal cord injury-induced rat glial scar.Bioengineering & translational medicine · 2025Article
- Pin1-catalyzed conformational regulation after phosphorylation: A distinct checkpoint in cell signaling and drug discovery.Science signaling · 2024Review
- Review
- New PIN1 inhibitors identified through a pharmacophore-driven, hierarchical consensus docking strategy.Journal of enzyme inhibition and medicinal chemistry · 2022Article
- Pin1 inhibition potently suppresses gastric cancer growth and blocks PI3K/AKT and Wnt/β-catenin oncogenic pathways.Molecular carcinogenesis · 2019Article
- Editorial: Peptidyl-Prolyl Isomerases in Human Pathologies.Frontiers in pharmacology · 2019Article
- Oncogenic Hijacking of the PIN1 Signaling Network.Frontiers in oncology · 2019Review
- A Guide to PIN1 Function and Mutations Across Cancers.Frontiers in pharmacology · 2018Article
- PIN1 in breast development and cancer: a clinical perspective.Cell death and differentiation · 2017Review
- G Protein-coupled Receptor Kinase 2 (GRK2) Promotes Breast Tumorigenesis Through a HDAC6-Pin1 Axis.EBioMedicine · 2016Article
- Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α.The Journal of biological chemistry · 2015Article
- Prolyl isomerase Pin1 in cancer.Cell research · 2014Review
- Diallyl trisulfide inhibits estrogen receptor-α activity in human breast cancer cells.Breast cancer research and treatment · 2014Article
- Links between oestrogen receptor activation and proteolysis: relevance to hormone-regulated cancer therapy.Nature reviews. Cancer · 2014Review
- Phosphorylation: a fundamental regulator of steroid receptor action.Trends in endocrinology and metabolism: TEM · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In hormone receptor-positive breast cancers, most tumors in the early stages of development depend on the activity of the estrogen receptor and its ligand, estradiol. Anti-estrogens, such as tamoxifen, have been used as the first line of therapy for over three decades due to the fact that they elicit cell cycle arrest. Unfortunately, after an initial period, most cells become resistant to hormonal therapy. Peptidylprolyl isomerase 1 (Pin1), a protein overexpressed in many tumor types including breast, has been demonstrated to modulate ERalpha activity and is involved in resistance to hormonal therapy. Here we show a new mechanism through which CDK2 drives an ERalpha-Pin1 interaction under hormone- and growth factor-free conditions. The PI3K/AKT pathway is necessary to activate CDK2, which phosphorylates ERalphaSer294, and mediates the binding between Pin1 and ERalpha. Site-directed mutagenesis demonstrated that ERalphaSer294 is essential for Pin1-ERalpha interaction and modulates ERalpha phosphorylation on Ser118 and Ser167, dimerization and activity. These results open up new drug treatment opportunities for breast cancer patients who are resistant to anti-estrogen therapy.
Indexed as
Identifiers
What OpenQuestion holds
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.