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

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Mylona, Anastasia | Theillet, Francois-Xavier | Foster, Charles | Cheng, Tammy, M | Miralles, Francesc | Bates, Paul, A | Selenko, Philipp | Treisman, Richard

Edité par CCSD ; American Association for the Advancement of Science (AAAS) -

International audience. A function for multisite phosphorylation Many transcription factors are regulated by phosphorylation on multiple residues. Mylona et al. analyzed multisite phosphorylation in the transcription factor Elk-1 and showed that it may protect against excessive activation (see the Perspective by Whitmarsh and Davis). Phosphorylation by the kinase ERK2 occurred at eight sites, but the sites were phosphorylated at different rates. Those that were phosphorylated more quickly promoted transcriptional activation. Those that were phosphorylated more slowly dampened excessive activation by ERK2s without needing a phosphatase or any other negative regulatory component. Science , this issue p. 233 ; see also p. 179

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