Rapid immunoprecipitation by mass spectrometry of endogenous...

created [InstanceEdit:9038160] Rothfels, Karen, 2018-02-23
dbId 9038162
displayName Rapid immunoprecipitation by mass spectrometry of endogenous...
schemaClass Summation
text Rapid immunoprecipitation by mass spectrometry of endogenous proteins (RIME) analysis shows that in addition to interacting with PGR after progesterone stimulation, ESR1 also interacts with known co-activators NRIP, GATA3 and TLE3 (Mohammed et al, 2013; Mohammed et al, 2015). Progesterone treatment of breast cancer cell lines under estrogen-rich conditions promotes a redistribution of ER alpha binding to PGR binding sites. This redistribution coincides with co-occupancy of FOXA1 and EP300 at the novel binding sites as well as with the H3K27Ac mark, suggesting that the binding events are functional (Clarke et al, 2012; Mohammed et al, 2015).
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