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Ubiquitin‐activating enzyme is necessary for 17β‐estradiol‐induced breast cancer cell proliferation and migration
Author(s) -
Pesiri Valeria,
Totta Pierangela,
Marino Maria,
Acconcia Filippo
Publication year - 2014
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1296
Subject(s) - protein kinase b , pi3k/akt/mtor pathway , cell growth , signal transduction , activator (genetics) , cell migration , microbiology and biotechnology , ubiquitin , mapk/erk pathway , estrogen receptor , chemistry , cancer research , biology , cell , breast cancer , receptor , cancer , biochemistry , genetics , gene
The sex steroid hormone 17β‐estradiol (E2) regulates breast cancer (BC) cell proliferation and migration through the activation of a plethora of signal transduction cascades ( e.g ., PI3K/AKT activation) starting after E2 binding to the estrogen receptor alpha (ERα). The activity of the ubiquitin (Ub)‐system modulates many physiological processes ( e.g ., cell proliferation and migration), and recently, a specific inhibitor (Pyr‐41) of the Ub‐activating enzyme (E 1 ), which works as the activator of the Ub‐based signaling, has been identified to prevent the functions of the Ub‐system. Here, by using Pyr‐41, we studied the involvement of the Ub‐system in E2‐induced signaling to proliferation and migration of BC cells. Our data indicate that E 1 activity is involved in the E2:ERα signaling important for cell proliferation and migration through the modulation of the E2‐evoked activation of the PI3K/AKT and the p38/MAPK pathways. These discoveries indicate a new molecular circuitry that can be further explored to define new opportunities for BC treatment. © 2014 IUBMB Life, 66(8):578–585, 2014