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Cited by 31Protein Kinase Regulation and GTPase SignalingProtein Structure and DynamicsProtein Tyrosine Phosphatases

The Third Conformation of p38α MAP Kinase Observed in Phosphorylated p38α and in Solution

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Akella, Radha, Min, Xiaoshan, Wu, Qiong, Gardner, Kevin H., Goldsmith, Elizabeth J.·2010·Structure
DOI 10.1016/j.str.2010.09.015
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Abstract

MAPKs engage substrates, MAP2Ks, and phosphatases via a docking groove in the C-terminal domain of the kinase. Prior crystallographic studies on the unphosphorylated MAPKs p38α and ERK2 defined the docking groove and revealed long-range conformational changes affecting the activation loop and active site of the kinase induced by peptide. Solution NMR data presented here for unphosphorylated p38α with a MEK3b-derived peptide (p38α/pepMEK3b) validate these findings. Crystallograhic data from doubly phosphorylated active p38α (p38α/T∗GY∗/pepMEK3b) reveal a structure similar to unphosphorylated p38α/MEK3b, and distinct from phosphorylated p38γ (p38γ/T∗GY∗) and ERK2 (ERK2/T∗EY∗). The structure supports the idea that MAP kinases adopt three distinct conformations: unphosphorylated, phosphorylated, and a docking peptide-induced form.

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  • Sequence-specific backbone assignment has been achieved for p38a (82%), activated pTpYp38a (56%), and ERK2 (65%), including key MAPK regulatory elements.

    “The basis of any NMR spectroscopy analysis is the sequence-specific backbone assignment, which has been achieved for p38a 47,58,61 (82%), activated pTpYp38a 69 (56%) and ERK2 65 (65%) and include key MAPK regulatory elements, especially the KIM binding pockets (93%/95% for p38a/ERK2) the glycine-rich loops (100%/100% for p38a/ERK2) and the activation loops (83%/none for p38a/ERK2).”

    From Molecular basis of MAP kinase regulation (2013) · cites this paper as [47]

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References 56 · Cited by 31

Authors
Akella, R., Min, X., Wu, Q., Gardner, K. H., & Goldsmith, E. J.
Affiliations
The University of Texas Southwestern Medical Center (US)
Corresponding author
Goldsmith, Elizabeth J.
ORCID
Venue
Structure
Publisher
Elsevier BV
Published
2010-12
Volume
18
Issue
12
Pages
1571-1578
ISSN
0969-2126 (ISSN-L)
DOI
10.1016/j.str.2010.09.015
OpenAlex
W1997653315
Cited by
31
References
56
Citations by year
2026: 1 · 2023: 2 · 2021: 2 · 2020: 1 · 2019: 5 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 2 · 2014: 2 · 2013: 4 · 2012: 3
FWCI
1.43
Type
journal article
Language
en
Open access
Licence
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 Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
p38α MAP kinase, phosphorylation, C-terminal domain, activation loop, ERK2, p38γ, kinase substrate recognition, solution structure
MeSH terms
Amino Acid Sequence, Animals, Binding Sites, Models, Biological, Models, Molecular, Molecular Sequence Data, Phosphorylation, Protein Binding, Solutions, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinase 14, Mice, Protein Interaction Domains and Motifs

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