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Identification of Antiestrogen‐Bound Estrogen Receptor α Interactomes in Hormone‐Responsive Human Breast Cancer Cell Nuclei
Author(s) -
Gigantino Valerio,
Salvati Annamaria,
Giurato Giorgio,
Palumbo Domenico,
Strianese Oriana,
Rizzo Francesca,
Tarallo Roberta,
Nyman Tuula A.,
Weisz Alessandro,
Nassa Giovanni
Publication year - 2020
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.202000135
Subject(s) - fulvestrant , antiestrogen , estrogen receptor , tamoxifen , estrogen , estrogen receptor alpha , selective estrogen receptor modulator , estrogen receptor beta , biology , transcription factor , proteomics , breast cancer , cancer research , cancer , endocrinology , biochemistry , genetics , gene
Estrogen receptor alpha (ERα) is a ligand‐inducible transcription factor which mediates estrogen actions in hormone‐responsive tumors and is targeted by effective anticancer therapies based on the ERα antagonist ligands, selective estrogen receptor modulators (such as Tamoxifen/TAM) or disruptors (such as Fulvestrant/ICI). Despite its importance for cancer therapy, including acquired resistance to endocrine therapy, the molecular basis of ERα response to different ligands is not fully known to date. Interaction proteomics shows great potential to identify and characterize molecular mechanisms of disease based on physical and functional protein‐protein interaction networks. Tandem affinity purification coupled to mass spectrometry is applied here for mapping in hormone‐responsive breast cancer cells nuclei, the ERα interactomes, induced by each of the two classes of antiestrogens. The results provide new insights on the molecular bases for antiestrogen‐mediated control of ERα function and reveal new potential ways to overcome endocrine therapy resistance in cancer.