Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2

Zhou, Tianjun; Sun, Liguang; Humphreys, John; Goldsmith, Elizabeth J.

doi:10.1016/j.str.2006.04.006

Cited by 165Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesMelanoma and MAPK Pathways

Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2

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Zhou, Tianjun, Sun, Liguang, Humphreys, John, Goldsmith, Elizabeth J.·2006·Structure

DOI 10.1016/j.str.2006.04.006

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Abstract

MAP kinases bind activating kinases, phosphatases, and substrates through docking interactions. Here, we report a 1.9 A crystallographic analysis of inactive ERK2 bound to a "D motif" docking peptide (pepHePTP) derived from hematopoietic tyrosine phosphatase, a negative regulator of ERK2. In this complex, the complete D motif interaction defined by mutagenic analysis is observed, including extensive electrostatic interactions with the "CD" site of the kinase. Large conformational changes occur in the activation loop where the dual phosphorylation sites, which are buried in the inactive form of ERK2, become exposed to solvent in the complex. Similar conformational changes occur in a complex between ERK2 and a MEK2 (MAP/ERK kinase-2)-derived D motif peptide (pepMEK2). D motif peptides are known to bind homologous loci in the MAP kinases p38alpha and JNK1, also inducing conformational changes in these enzymes. However, the binding interactions and conformational changes are unique to each, thus contributing to specificity among MAP kinases.

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KIM sequences that contain conserved basic and hydrophobic residues, and are part of the well-folded MKBD of typical DUSPs, engage the common complementary KIM-binding groove in MAPKs.
“It was hypothesized that the KIM sequences that contain conserved basic and hydrophobic residues, and are part of the well-folded MKBD of the typical DUSPs, engage the common complementary KIM-binding groove in MAPKs.41,44 This was only recently confirmed”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [44]
MAPK docking is a well-characterized protein-peptide interaction system.
“At the structural level, MAPK docking is a well characterized protein-peptide interaction system (9, 12-16).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [12]
Docking motifs from HePTP, MEF2A, and NFAT4 bind the MAPK docking groove.
“Docking motifs from these three proteins bind the MAPK docking groove (9,12,22).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [12]

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Authors: Zhou, T., Sun, L., Humphreys, J., & Goldsmith, E. J.
Affiliations: The University of Texas Southwestern Medical Center (US)
China Medical University (CN)
Corresponding author: Goldsmith, Elizabeth J.
ORCID: Humphreys, John
Goldsmith, Elizabeth J.
Venue: Structure
Publisher: Elsevier BV
Published: 2006-06
Volume: 14
Issue: 6
Pages: 1011-1019
ISSN: 0969-2126 (ISSN-L)
DOI: 10.1016/j.str.2006.04.006
OpenAlex: W2001183750
Cited by: 164
References: 37
Citations by year: 2026: 7 · 2025: 1 · 2024: 4 · 2023: 7 · 2022: 3 · 2021: 2 · 2020: 5 · 2019: 5 · 2018: 2 · 2017: 8 · 2016: 13 · 2015: 10 · 2014: 5 · 2013: 9 · 2012: 13
FWCI: 6.11
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2639 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Structure (publishedVersion)
PubMed (publishedVersion)
OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
Funders: Welch Foundation
Biological and Environmental Research (W-31-109-ENG-38)
National Institutes of Health (DK46993, I1128)
Argonne National Laboratory
U.S. Department of Energy
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 Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Keywords: ERK2, mitogen-activated protein kinase, MEK2, electrostatic interactions, kinase regulation, p38α, JNK1
MeSH terms: Amino Acid Sequence, Animals, Enzyme Activation, Molecular Sequence Data, Protein Conformation, Protein Tyrosine Phosphatases, Mitogen-Activated Protein Kinase 1, Amino Acid Motifs, Protein Interaction Mapping, Intracellular Signaling Peptides and Proteins, Protein Tyrosine Phosphatase, Non-Receptor Type 6

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Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2

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