Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation

@article{Mylona2016OpposingEO,
  title={Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation},
  author={Anastasia Mylona and Franco̧is-Xavier Theillet and Charles Foster and Tammy M. K. Cheng and Francesc Miralles and Paul A. Bates and Philipp Selenko and Richard Treisman},
  journal={Science},
  year={2016},
  volume={354},
  pages={233-237}
}
  • Anastasia Mylona, Franco̧is-Xavier Theillet, +5 authors Richard Treisman
  • Published in Science 2016
  • Biology, Medicine
  • Multisite phosphorylation regulates many transcription factors, including the serum response factor partner Elk-1. Phosphorylation of the transcriptional activation domain (TAD) of Elk-1 by the protein kinase ERK at multiple sites potentiates recruitment of the Mediator transcriptional coactivator complex and transcriptional activation, but the roles of individual phosphorylation events had remained unclear. Using time-resolved nuclear magnetic resonance spectroscopy, we found that ERK2… CONTINUE READING

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