Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, deoxyribonucleic acid, and coregulators associated with alterations in estrogen and tamoxifen activity.

@article{Likhite2006KinasespecificPO,
  title={Kinase-specific phosphorylation of the estrogen receptor changes receptor interactions with ligand, deoxyribonucleic acid, and coregulators associated with alterations in estrogen and tamoxifen activity.},
  author={Varsha S. Likhite and Fabio Stossi and Kyuri Kim and Benita S Katzenellenbogen and John A. Katzenellenbogen},
  journal={Molecular endocrinology},
  year={2006},
  volume={20 12},
  pages={3120-32}
}
Posttranslational modifications of the estrogen receptor (ER) are emerging as important regulatory elements of cross talk between different signaling pathways. ER phosphorylation, in particular, has been implicated in the ligand-independent effects of ER and in tamoxifen resistance of breast tumors. In our studies, Western immunoblot analysis of endogenous ER in parental MCF-7 cells reveals specific, ligand-dependent phosphorylations at S118 and S167, with this ligand dependence being lost in… CONTINUE READING

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