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A large set of estrogen receptor β‐interacting proteins identified by tandem affinity purification in hormone‐responsive human breast cancer cell nuclei
Author(s) -
Nassa Giovanni,
Tarallo Roberta,
Ambrosino Concetta,
Bamundo Angela,
Ferraro Lorenzo,
Paris Ornella,
Ravo Maria,
Guzzi Pietro H.,
Cannataro Mario,
Baumann Marc,
Nyman Tuula A.,
Nola Ernesto,
Weisz Alessandro
Publication year - 2010
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.201000344
Subject(s) - estrogen receptor , breast cancer , human breast , receptor , biology , computational biology , cancer , chemistry , microbiology and biotechnology , biochemistry , genetics
Estrogen receptors α (ER‐α) and β (ER‐β) play distinct biological roles in onset and progression of hormone‐responsive breast cancer, with ER‐β exerting a modulatory activity on ER‐α‐mediated estrogen signaling and stimulation of cell proliferation by mechanisms still not fully understood. We stably expressed human ER‐β fused to a tandem affinity purification‐tag in estrogen‐responsive MCF‐7 cells and applied tandem affinity purification and nanoLC‐MS/MS to identify the ER‐β interactome of this cell type. Functional annotation by bioinformatics analyses of the 303 proteins that co‐purify with ER‐β from nuclear extracts identify several new molecular partners of this receptor subtype that represents nodal points of a large protein network controlling multiple processes and functions in breast cancer cells.