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The mechanism of phosphorylation-inducible activation of the ETS-domain transcription factor Elk-1

Lookup NU author(s): Professor Jeremy Lakey

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Abstract

Protein phosphorylation represents one of the major mechanisms for transcription factor activation. Here we demonstrate a molecular mechanism by which phosphorylation by mitogen-activated protein (MAP) kinases leads to changes in transcription factor activity. MAP kinases stimulate DNA binding and transcriptional activation mediated by the mammalian ETS-domain transcription factor Elk-1. Phosphorylation of the C-terminal transcriptional activation domain induces a conformational change in Elk-1, which accompanies the stimulation of DNA binding. C-terminal phosphorylation is coupled to activation Of DNA binding by the N-terminal DNA-binding domain via an additional intermediary domain. Activation of DNA binding is mediated by an allosteric mechanism involving the key phosphoacceptor residues. Together, these results provide a molecular model for how phosphorylation induces changes in Elk-1 activity.


Publication metadata

Author(s): Lakey JH; Yang SH; Shore P; Willingham N; Sharrocks AD

Publication type: Article

Publication status: Published

Journal: EMBO Journal

Year: 1999

Volume: 18

Issue: 20

Pages: 5666-5674

Print publication date: 01/10/1999

ISSN (print): 0261-4189

ISSN (electronic): 1460-2075

Publisher: Nature Publishing Group

URL: http://dx.doi.org/10.1093/emboj/18.20.5666

DOI: 10.1093/emboj/18.20.5666


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