ReviewMolecular and cellular endocrinology2019
Insights into how phosphorylation of estrogen receptor at serine 305 modulates tamoxifen activity in breast cancer.
Review in Molecular and cellular endocrinology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Crosstalk between SUMOylation and other post-translational modifications in breast cancer.Cellular & molecular biology letters · 2024Review
- Tailoring Potential Natural Compounds for the Treatment of Luminal Breast Cancer.Pharmaceuticals (Basel, Switzerland) · 2023Review
- CRISPR-Cas9 screen reveals a role of purine synthesis for estrogen receptor α activity and tamoxifen resistance of breast cancer cells.Science advances · 2023Article
- BAP18 facilitates CTCF-mediated chromatin accessible to regulate enhancer activity in breast cancer.Cell death and differentiation · 2023Article
- Non-Coding RNAs Modulating Estrogen Signaling and Response to Endocrine Therapy in Breast Cancer.Cancers · 2023Review
- Hyperactivation of p21-Activated Kinases in Human Cancer and Therapeutic Sensitivity.Biomedicines · 2023Review
- Posttranslational control of lipogenesis in the tumor microenvironment.Journal of hematology & oncology · 2022Review
- Membrane-Initiated Estrogen, Androgen, and Progesterone Receptor Signaling in Health and Disease.Endocrine reviews · 2022Review
- 90 YEARS OF PROGESTERONE: Steroid receptors as MAPK signaling sensors in breast cancer: let the fates decide.Journal of molecular endocrinology · 2020Review
- Preparation, Characterization, and Pharmacokinetic Study of a Novel Long-Acting Targeted Paclitaxel Liposome with Antitumor Activity.International journal of nanomedicine · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Estrogen receptor (ER) is the most important factor in the pathophysiology of breast cancer. Consequently, modulation of ER activity has been exploited to develop drugs against ER + breast cancer, such as tamoxifen, referred to as endocrine therapies. With deeper understanding of ER mechanism of action, posttranslational modifications (PTMs) are increasingly recognized as important in mediating ER activity. Some ER PTMs such as phosphorylation, are studied in the context of ligand-independent ER activity. However, they also play a pivotal role in defining the actions and outcome of the antiestrogen-bound ER. The complexity of these actions is increasing as new PTMs are identified, yet the functional consequences and clinical implications are not fully understood. This review will examine and summarize new emerging mechanistic knowledge and clinical data in breast cancer on how these PTMs affect antiestrogen-ER activity, with an emphasis on phosphorylation of serine 305 (S305). This phosphorylation site represents an integrated hub of oncogenic signaling to modulate ER conformation, dimerization, coregulators, and DNA binding to profoundly reduce sensitivity to endocrine therapy. Consequently, (i) S305 has the potential to become a useful marker of tamoxifen response, and (ii) blocking S305 phosphorylation defines a new therapeutic strategy to overcome tamoxifen resistance in breast cancer.
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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.