Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
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The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded, bringing the phosphothreonine and phosphotyrosine into alignment with surface arginine-rich binding sites. Conformational changes occur in the lip and neighboring structures, including the P+1 site, the MAP kinase insertion, the C-terminal extension, and helix C. Domain rotation and remodeling of the proline-directed P+1 specificity pocket account for the activation. The conformation of the P+1 pocket is similar to a second proline-directed kinase, CDK2-CyclinA, thus permitting the origin of this specificity to be defined. Conformational changes outside the lip provide loci at which the state of phosphorylation can be felt by other cellular components.
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ERK phospho-Tyr185 binds in a positively charged C-lobe pocket, where it appears to anchor and limit activation-loop flexibility.
“ERK phospho-Tyr185 binds in a positively charged pocket in the C-lobe, where it appears to act as an anchor to limit flexibility of the A-loop (Canagarajah et al., 1997).”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Canagarajah et al., 1997
In active ERK, phospho-Thr183 binds under αC to a highly positively charged pocket in the N-lobe.
“The phospho-Thr183 of ERK binds under the αC to a highly positively charged pocket in the N-lobe (Figure 4D).”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Canagarajah et al., 1997
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“To understand why the mutations block hinge, but not rotation motion, we compared the active, phosphorylated ERK structure (Canagarajah et al., 1997) with the mutant JNK1 structures.”
BackgroundMae inhibits Pointed‐P2 transcriptional activity by blocking its MAPK docking site
Qiao, F., Harada, B., Song, H., Whitelegge, J., Courey, A. J., & Bowie, J. U. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600924 · Cited by 41 · see citing works
Understanding the specificity of a docking interaction between JNK1 and the scaffolding protein JIP1
Yan, C., Kaoud, T., Lee, S., Dalby, K. N., & Ren, P. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp1073522 · Cited by 36 · see citing works
Tárrega, C., Blanco-Aparicio, C., Muñoz, J. J., & Pulido, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108874200 · Cited by 33 · see citing works
Resting and Active States of the ERK2:HePTP Complex
Francis, D. M., Różycki, B., Tortajada, A., Hummer, G., Peti, W., & Page, R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2075136 · Cited by 32 · see citing works
The Third Conformation of p38α MAP Kinase Observed in Phosphorylated p38α and in Solution
Akella, R., Min, X., Wu, Q., Gardner, K. H., & Goldsmith, E. J. (2010) · Structure · doi:10.1016/j.str.2010.09.015 · Cited by 31 · see citing works
Self-citationMa, W., Shang, Y., Wei, Z., Wen, W., Wang, W., & Zhang, M. (2010) · Structure · doi:10.1016/j.str.2010.08.011 · Cited by 31 · see citing works
Structural Basis of Substrate Recognition by Hematopoietic Tyrosine Phosphatase,
Critton, D. A., Tortajada, A., Stetson, G., Peti, W., & Page, R. (2008) · Biochemistry · doi:10.1021/bi801724n · Cited by 28 · see citing works
Lee, S., Warthaka, M., Yan, C., Kaoud, T. S., Piserchio, A., Ghose, R., Ren, P., & Dalby, K. N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018594 · Cited by 26 · see citing works
Molecular Determinants of Substrate Recognition in Hematopoietic Protein-tyrosine Phosphatase
Huang, Z., Zhou, B., & Zhang, Z.-Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407820200 · Cited by 23 · see citing works
NMR Spectroscopic Investigations of the Activated p38α Mitogen‐Activated Protein Kinase
Nielsen, G., & Schwalbe, H. (2011) · ChemBioChem · doi:10.1002/cbic.201100527 · Cited by 15 · see citing works
- Authors
- Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Goldsmith, Elizabeth J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-09
- Volume
- 90
- Issue
- 5
- Pages
- 859-869
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2140490890
- Cited by
- 729
- References
- 75
- Citations by year
- 2026: 15 · 2025: 9 · 2024: 13 · 2023: 16 · 2022: 10 · 2021: 12 · 2020: 19 · 2019: 19 · 2018: 13 · 2017: 18 · 2016: 19 · 2015: 23 · 2014: 23 · 2013: 18 · 2012: 24
- FWCI
- 12.33
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 46993, R01DK046993)
- 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 › Protein Structure and Dynamics
- Keywords
- ERK2, MAPK activation, dual phosphorylation, phosphothreonine, phosphotyrosine, conformational change, domain rotation, kinase specificity, protein structure
- MeSH terms
- Binding Sites, Crystallography, Enzyme Activation, Molecular Sequence Data, Phosphorylation, Proline, Protein Conformation, Substrate Specificity, Threonine, Tyrosine, Protein Structure, Secondary, Protein Structure, Tertiary, Calcium-Calmodulin-Dependent Protein Kinases, Dimerization, Mitogen-Activated Protein Kinase 1
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