Recognition of ERK MAP kinase by PEA‐15 reveals a common docking site within the death domain and death effector domain

Hill, Justine M.; Vaidyanathan, Hema; Ramos, Joe W.; Ginsberg, Mark H.; Werner, Milton H.

doi:10.1093/emboj/cdf641

Cited by 101Protein Kinase Regulation and GTPase SignalingProtein Structure and DynamicsMelanoma and MAPK Pathways

Recognition of ERK MAP kinase by PEA‐15 reveals a common docking site within the death domain and death effector domain

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Hill, Justine M., Vaidyanathan, Hema, Ramos, Joe W., Ginsberg, Mark H., Werner, Milton H.·2002·The EMBO Journal

DOI 10.1093/emboj/cdf641PMC PMC136945

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Abstract

PEA-15 is a multifunctional protein that modulates signaling pathways which control cell proliferation and cell death. In particular, PEA-15 regulates the actions of the ERK MAP kinase cascade by binding to ERK and altering its subcellular localization. The three-dimensional structure of PEA-15 has been determined using NMR spectroscopy and its interaction with ERK defined by characterization of mutants that modulate ERK function. PEA-15 is composed of an N-terminal death effector domain (DED) and a C-terminal tail of irregular structure. NMR 'footprinting' and mutagenesis identified elements of both the DED and tail that are required for ERK binding. Comparison of the DED-binding surface for ERK2 with the death domain (DD)-binding surface of Drosophila Tube revealed an unexpected similarity between the interaction modes of the DD and DED motifs in these proteins. Despite a lack of functional or sequence similarity between PEA-15 and Tube, these proteins utilize a common surface of the structurally similar DD and DED to recognize functionally diverse targets.

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MAPK scaffolding proteins JIP1 and PEA-15 and substrates RSK1, MK2, and MEF2a also contain a linear KIM domain that mediates MAPK binding in the cell.
“Notably, MAPK scaffolding proteins (JNK-interacting protein, JIP1; 29 phosphoprotein enriched in astrocytes 15, PEA-15 30 ) and substrates (Ribosomal protein S6 kinase alpha-1, RSK1; 31 MAP kinase-activated protein kinase 2, MK2; 32 and myocyte enhancer factor 2A, MEF2a 33 ) also contain linear KIM domain, which mediates MAPK binding in the cell.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [30]

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Authors: Hill, J. M., Vaidyanathan, H., Ramos, J. W., Ginsberg, M. H., & Werner, M. H.
Affiliations: Rockefeller University (US)
Rutgers, The State University of New Jersey (US)
Scripps Research Institute (US)
Corresponding author: Werner, Milton H.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2002-12-01
Volume: 21
Issue: 23
Pages: 6494-6504
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/cdf641
PMC: PMC136945
OpenAlex: W2135553994
Cited by: 100
References: 60
Citations by year: 2026: 1 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 1 · 2021: 2 · 2019: 2 · 2018: 1 · 2016: 2 · 2015: 5 · 2014: 4 · 2013: 7 · 2012: 6
FWCI: 2.90
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute (R01CA093849)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Keywords: PEA-15, ERK MAP kinase, ERK2, death effector domain, death domain, protein-protein interaction, docking site, subcellular localization, cell death signaling, protein structure
MeSH terms: Amino Acid Sequence, Animals, Epitopes, Binding Sites, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Phosphoproteins, Protein Binding, Sequence Alignment, Protein Structure, Tertiary, Amino Acid Motifs, Mitogen-Activated Protein Kinases, Apoptosis Regulatory Proteins, Mice

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Recognition of ERK MAP kinase by PEA‐15 reveals a common docking site within the death domain and death effector domain

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