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

Author:

Mylona Anastasia1,Theillet Francois-Xavier2,Foster Charles1,Cheng Tammy M.3,Miralles Francesc14,Bates Paul A.3,Selenko Philipp2,Treisman Richard1

Affiliation:

1. Signalling and Transcription Laboratory, Francis Crick Institute, Lincoln’s Inn Fields Laboratory, London WC2A 3LY, UK.

2. In-Cell NMR Laboratory, Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Berlin, Germany.

3. Biomolecular Modelling Laboratory, Francis Crick Institute, Lincoln’s Inn Fields Laboratory, London WC2A 3LY, UK.

4. Molecular & Clinical Sciences Research Institute, St. George’s, University of London, London SW17 0RE, UK.

Abstract

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

Funder

Francis Crick Institute

Cancer Research UK

UK Medical Research Council

Wellcome Trust

European Research Council (ERC)

ERC

Agence Nationale pour la Recherche

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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