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Sci. Signal., 25 October 2011
Vol. 4, Issue 196, p. rs11
[DOI: 10.1126/scisignal.2002010]


Editor's Summary

Discovering ERK2 Substrates
Extracellular signal–regulated kinase 2 (ERK2) is one of two closely related mitogen-activated protein kinases (MAPKs) that function downstream of many receptors. Because ERK2 and ERK1 are usually activated under the same conditions and are recognized by the same antibodies, it can be difficult to assign specific substrates and functions to these related proteins. Carlson et al. combined mass spectrometry analysis with chemical genetics to identify ERK2-specific substrates. Their work identified targets in diverse pathways suggesting mechanisms for crosstalk with MAPK signaling. Additionally, detailed analysis of the transcriptional repressor ETV3 suggested that phosphorylation by ERK2 on sites in both canonical and noncanonical motifs inhibited its DNA binding capacity, which may poise cells for a transient transcriptional burst in response to stimuli that activate ERK signaling or those that arrive concurrently.

Citation: S. M. Carlson, C. R. Chouinard, A. Labadorf, C. J. Lam, K. Schmelzle, E. Fraenkel, F. M. White, Large-Scale Discovery of ERK2 Substrates Identifies ERK-Mediated Transcriptional Regulation by ETV3. Sci. Signal. 4, rs11 (2011).

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Phosphoproteome dynamics reveal novel ERK1/2 MAP kinase substrates with broad spectrum of functions.
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A developmentally regulated translational control pathway establishes the meiotic chromosome segregation pattern.
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ERF and ETV3L are retinoic acid-inducible repressors required for primary neurogenesis.
A. Janesick, R. Abbey, C. Chung, S. Liu, M. Taketani, and B. Blumberg (2013)
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DEF Pocket in p38{alpha} Facilitates Substrate Selectivity and Mediates Autophosphorylation.
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J. Biol. Chem. 288, 18407-18420
   Abstract »    Full Text »    PDF »
Kinase-Substrate Enrichment Analysis Provides Insights into the Heterogeneity of Signaling Pathway Activation in Leukemia Cells.
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Cyclic GMP-dependent Stimulation of Serotonin Transport Does Not Involve Direct Transporter Phosphorylation by cGMP-dependent Protein Kinase.
A. Wong, Y.-W. Zhang, G. R. Jeschke, B. E. Turk, and G. Rudnick (2012)
J. Biol. Chem. 287, 36051-36058
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Mitogen-Activated Protein Kinase Phosphorylation of Splicing Factor 45 (SPF45) Regulates SPF45 Alternative Splicing Site Utilization, Proliferation, and Cell Adhesion.
A. M. Al-Ayoubi, H. Zheng, Y. Liu, T. Bai, and S. T. Eblen (2012)
Mol. Cell. Biol. 32, 2880-2893
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Labeling and Identification of Direct Kinase Substrates.
S. M. Carlson and F. M. White (2012)
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ROCK in a Stiff Place.
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