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

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 c... Full description

Journal Title: Science (New York N.Y.), October 14, 2016, Vol.354(6309), pp.233-237
Main Author: Mylona, Anastasia
Other Authors: Theillet, Francois-Xavier , Foster, Charles , Cheng, Tammy M , Miralles, Francesc , Bates, Paul A , Selenko, Philipp , Treisman, Richard
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1095-9203
Link: http://search.proquest.com/docview/1835418310/?pq-origsite=primo
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recordid: proquest1835418310
title: Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation.
format: Article
creator:
  • Mylona, Anastasia
  • Theillet, Francois-Xavier
  • Foster, Charles
  • Cheng, Tammy M
  • Miralles, Francesc
  • Bates, Paul A
  • Selenko, Philipp
  • Treisman, Richard
subjects:
  • Animals–Metabolism
  • Enzyme Activation–Metabolism
  • Gene Expression Regulation–Chemistry
  • Humans–Genetics
  • MAP Kinase Signaling System–Metabolism
  • Mice–Metabolism
  • Mitogen-Activated Protein Kinase 1–Metabolism
  • Mutagenesis–Metabolism
  • Nuclear Magnetic Resonance, Biomolecular–Metabolism
  • Phosphorylation–Metabolism
  • Protein Domains–Metabolism
  • Serum Response Factor–Metabolism
  • Ets-Domain Protein Elk-1–Metabolism
  • Serum Response Factor
  • Ets-Domain Protein Elk-1
  • Mitogen-Activated Protein Kinase 1
ispartof: Science (New York, N.Y.), October 14, 2016, Vol.354(6309), pp.233-237
description: 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 phosphorylation proceeds at markedly different rates at eight TAD sites in vitro, which we classified as fast, intermediate, and slow. Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output. Progressive Elk-1 phosphorylation thus ensures a self-limiting response to ERK activation, which occurs independently of antagonizing phosphatase activity. 10.1126/science.aad1872
language: eng
source:
identifier: E-ISSN: 1095-9203
fulltext: no_fulltext
issn:
  • 10959203
  • 1095-9203
url: Link


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titleOpposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation.
creatorMylona, Anastasia ; Theillet, Francois-Xavier ; Foster, Charles ; Cheng, Tammy M ; Miralles, Francesc ; Bates, Paul A ; Selenko, Philipp ; Treisman, Richard
contributorMylona, Anastasia (correspondence author) ; Mylona, Anastasia (record owner)
ispartofScience (New York, N.Y.), October 14, 2016, Vol.354(6309), pp.233-237
identifierE-ISSN: 1095-9203
subjectAnimals–Metabolism ; Enzyme Activation–Metabolism ; Gene Expression Regulation–Chemistry ; Humans–Genetics ; MAP Kinase Signaling System–Metabolism ; Mice–Metabolism ; Mitogen-Activated Protein Kinase 1–Metabolism ; Mutagenesis–Metabolism ; Nuclear Magnetic Resonance, Biomolecular–Metabolism ; Phosphorylation–Metabolism ; Protein Domains–Metabolism ; Serum Response Factor–Metabolism ; Ets-Domain Protein Elk-1–Metabolism ; Serum Response Factor ; Ets-Domain Protein Elk-1 ; Mitogen-Activated Protein Kinase 1
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descriptionMultisite 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 phosphorylation proceeds at markedly different rates at eight TAD sites in vitro, which we classified as fast, intermediate, and slow. Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output. Progressive Elk-1 phosphorylation thus ensures a self-limiting response to ERK activation, which occurs independently of antagonizing phosphatase activity. 10.1126/science.aad1872
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titleOpposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation.
authorMylona, Anastasia ; Theillet, Francois-Xavier ; Foster, Charles ; Cheng, Tammy M ; Miralles, Francesc ; Bates, Paul A ; Selenko, Philipp ; Treisman, Richard
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