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mTOR/S6K1 and MAPK/RSK signaling pathways coordinately regulate estrogen receptor α serine 167 phosphorylation
Author(s) -
Yamnik Rachel L.,
Holz Marina K.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.11.041
Subject(s) - phosphorylation , p70 s6 kinase 1 , estrogen receptor , pi3k/akt/mtor pathway , cancer research , mapk/erk pathway , signal transduction , estrogen , serine , breast cancer , estrogen receptor alpha , microbiology and biotechnology , biology , chemistry , cancer , medicine , endocrinology
Resistance to anti‐estrogen therapy is a major clinical concern in treatment of breast cancer. Estrogen‐independent phosphorylation of estrogen receptor α, specifically on Ser167, is one of the contributing causes to development of resistance, and a prognostic marker for the disease. Here, we dissect the signaling pathways responsible for Ser167 phosphorylation. We report that the mTOR/S6K1 and MAPK/RSK contribute non‐overlapping inputs into ERα activation via Ser167 phosphorylation. This cooperation may be targeted in breast cancer treatment by a combination of mTOR and MAPK inhibitors.