Activating ESR1 mutations in hormone-resistant metastatic breast cancer
Dan R. Robinson,Yi-Mi Wu,Pankaj Vats,Fengyun Su,Robert J. Lonigro,Xuhong Cao,Shanker Kalyana-Sundaram,Rui Wang,Yu Ning,Lynda Hodges,Amy Gursky,Javed Siddiqui,Scott A. Tomlins,Sameek Roychowdhury,Kenneth J. Pienta,Scott Y. H. Kim,J. Scott Roberts,James M. Rae,Catherine Van Poznak,Daniel F. Hayes,Rashmi Chugh,Lakshmi P. Kunju,Moshe Talpaz,Anne F. Schott,Arul M. Chinnaiyan +24 more
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TLDR
Five new LBD-localized ESR1 mutations identified here were shown to result in constitutive activity and continued responsiveness to anti-estrogen therapies in vitro, suggesting that activating mutations in E SR1 are a key mechanism in acquired endocrine resistance in breast cancer therapy.Abstract:
Arul Chinnaiyan and colleagues report the results of prospective clinical sequencing of 11 estrogen receptor–positive metastatic breast cancers. They identify ESR1 mutations affecting the ligand-binding domain in six hormone-resistant metastatic breast cancers and show that the mutant estrogen receptors are constitutively active and continue to be responsive to anti-estrogen therapies in vitro. Breast cancer is the most prevalent cancer in women, and over two-thirds of cases express estrogen receptor-α (ER-α, encoded by ESR1). Through a prospective clinical sequencing program for advanced cancers, we enrolled 11 patients with ER-positive metastatic breast cancer. Whole-exome and transcriptome analysis showed that six cases harbored mutations of ESR1 affecting its ligand-binding domain (LBD), all of whom had been treated with anti-estrogens and estrogen deprivation therapies. A survey of The Cancer Genome Atlas (TCGA) identified four endometrial cancers with similar mutations of ESR1. The five new LBD-localized ESR1 mutations identified here (encoding p.Leu536Gln, p.Tyr537Ser, p.Tyr537Cys, p.Tyr537Asn and p.Asp538Gly) were shown to result in constitutive activity and continued responsiveness to anti-estrogen therapies in vitro. Taken together, these studies suggest that activating mutations in ESR1 are a key mechanism in acquired endocrine resistance in breast cancer therapy.read more
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Androgen Receptor Is a Non-canonical Inhibitor of Wild-Type and Mutant Estrogen Receptors in Hormone Receptor-Positive Breast Cancers
Suriyan Ponnusamy,Sarah Asemota,Lee S. Schwartzberg,Fouzia Guestini,Keely May McNamara,Mariaelena Pierobon,Alba Font-Tello,Xintao Qiu,Yingtian Xie,Prakash Rao,Thirumagal Thiyagarajan,Brandy Grimes,Daniel L. Johnson,Martin D. Fleming,Frances E. Pritchard,Michael P Berry,Roy Oswaks,Richard E. Fine,Myles Brown,Hironobu Sasano,Emanuel F. Petricoin,Henry W. Long,Ramesh Narayanan +22 more
TL;DR: It is suggested that ligand-activated AR may function as a non-canonical inhibitor of ER and that AR agonists may offer a safe and effective treatment for ER-positive breast cancer.
Journal ArticleDOI
Hypoxia and Hormone-Mediated Pathways Converge at the Histone Demethylase KDM4B in Cancer.
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Journal ArticleDOI
Targeted mutation detection in breast cancer using MammaSeq
Nicholas G. Smith,Rekha Gyanchandani,Osama Shiraz Shah,Grzegorz T. Gurda,Peter C. Lucas,Ryan J. Hartmaier,Adam Brufsky,Shannon Puhalla,Amir Bahreini,Karthik Kota,Abigail I. Wald,Yuri E. Nikiforov,Marina N. Nikiforova,Steffi Oesterreich,Adrian V. Lee +14 more
TL;DR: MammaSeq is a targeted panel suitable for clinically actionable mutation detection in breast cancer, targeting 79 genes and 1369 mutations, optimized for use in primary and metastatic breast cancer.
Journal ArticleDOI
Targeting the IRE1-XBP1 axis to overcome endocrine resistance in breast cancer: Opportunities and challenges.
TL;DR: New insights are highlighted into the mechanisms of crosstalk between XBP1 and ER signaling and its clinical implications and the current state and future directions for targeting X BP1 in combination with standard endocrine therapy to improve clinical outcomes in endocrine-resistant breast cancer patients.
Journal ArticleDOI
The Phosphorylated Estrogen Receptor α (ER) Cistrome Identifies a Subset of Active Enhancers Enriched for Direct ER-DNA Binding and the Transcription Factor GRHL2.
Kyle T Helzer,Mary Szatkowski Ozers,Mark B. Meyer,Nancy A. Benkusky,Natalia M. Solodin,Rebecca Reese,Christopher L. Warren,J. Wesley Pike,Elaine T. Alarid +8 more
TL;DR: Results indicate that phosphorylation of ER at serine 118 promotes direct DNA binding at active enhancers and is a distinguishing mark for associated transcription factor complexes on chromatin.
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