The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry
Open accessAbstract
Protein interactions between MAP kinases and substrates, activators, and scaffolding proteins are regulated by docking site motifs, one containing basic residues proximal to Leu-X-Leu (DEJL) and a second containing Phe-X-Phe (DEF). Hydrogen exchange mass spectrometry was used to identify regions in MAP kinases protected from solvent by docking motif interactions. Protection by DEJL peptide binding was observed in loops spanning beta7-beta8 and alphaD-alphaE in p38alpha and ERK2. In contrast, protection by DEF binding to ERK2 revealed a distinct hydrophobic pocket for Phe-X-Phe binding formed between the P+1 site, alphaF helix, and the MAP kinase insert. In inactive ERK2, this pocket is occluded by intramolecular interactions with residues in the activation lip. In vitro assays confirm the dependence of Elk1 and nucleoporin binding on ERK2 phosphorylation, and provide a structural basis for preferential involvement of active ERK in substrate binding and nuclear pore protein interactions.
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“This supports the results of earlier H/D-MS studies from the Ahn laboratory that show the dynamics of key loops are affected be the interactions of MAPKs with peptides and ligands.66”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [66]
In the citing paper
“Allostery among the catalytic site, A-loop, and peptide-docking site of ERK and p38 MAPKs has been well documented (Chang et al., 2002; Goldsmith, 2011; Lee et al., 2004; Wang et al., 1997; Zhang et al., 1994; Zhou et al., 2006a, 2006b), but much less is known about these processes for JNK.”
From Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases (2012) · cites this paper as Lee et al., 2004
In the citing paper
“Moreover, the existence of FxFP (Phe-any amino acid-Phe-Pro) motifs in certain MAPK (especially ERK) substrates and a separate docking groove for such motifs on ERK suggest that in some cases two docking grooves on ERK may operate in combination: Elk1 for example contains both an FxFP and a D-motif (35-37).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [35]
Citations
Cites
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
Bmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARFPreprint
Jacobs, J. J. L., Scheijen, B., Voncken, J. W., Kieboom, K., Berns, A. J. M., & van Lohuizen, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2678 · Cited by 1,069
Molecular interpretation of ERK signal duration by immediate early gene products
Murphy, L. O., Smith, S. W., Chen, R., Fingar, D. C., & Blenis, J. (2002) · Nature Cell Biology · doi:10.1038/ncb822 · Cited by 928
A conserved docking motif in MAP kinases common to substrates, activators and regulators
Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E. (2000) · Nature Cell Biology · doi:10.1038/35000065 · Cited by 816
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729
Self-citationPhosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation
Khokhlatchev, A. V., Canagarajah, B. J., Wilsbacher, J. L., Robinson, M. J., Atkinson, M. A., Goldsmith, E. J., & Cobb, M. H. (1998) · Cell · doi:10.1016/s0092-8674(00)81189-7 · Cited by 675
Self-citationKallunki, T., Su, B., Tsigelny, I., Sluss, H. K., Dérijard, B., Moore, G., Davis, R., & Karin, M. (1994) · Genes & Development · doi:10.1101/gad.8.24.2996 · Cited by 642
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592
Self-citationThe JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins
Yasuda, J., Whitmarsh, A. J., Cavanagh, J., Sharma, M., & Davis, R. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.7245 · Cited by 458
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Jang, Y., Kim, M. A., & Kim, Y. (2017) · IET Systems Biology · doi:10.1049/iet-syb.2016.0042 · Cited by 1
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Xie, Q. (2014) · Iowa State University Digital Repository (Iowa State University) · doi:10.31274/etd-180810-83
Donohoe, G. C. (2016) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.5505 · Cited by 1
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Andreotti, A. H. (2023) · eLife · doi:10.7554/elife.91507.1.sa3
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Self-citationOrand, T., Delaforge, E., Chenal, M., Tengo, M., Herrmann, T., Cortés, J., Bernadó, P., & Jensen, M. R. (2025) · Advanced Science · doi:10.1002/advs.202503987
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Metadata
- Authors
- Lee, T., Hoofnagle, A. N., Kabuyama, Y., Stroud, J., Min, X., Goldsmith, E. J., Chen, L., Resing, K. A., & Ahn, N. G.
- Affiliations
- University of Colorado Boulder (US)
- Howard Hughes Medical Institute (US)
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Ahn, Natalie G
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2004-04
- Volume
- 14
- Issue
- 1
- Pages
- 43-55
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2020513008
- Cited by
- 282
- References
- 35
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 5 · 2023: 12 · 2022: 8 · 2021: 8 · 2020: 11 · 2019: 9 · 2018: 10 · 2017: 11 · 2016: 17 · 2015: 14 · 2014: 9 · 2013: 9 · 2012: 15
- FWCI
- 9.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM064642, R01-GM48521, R01GM048521)
- National Institute of Allergy and Infectious Diseases (R21AI049905)
- 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 › Melanoma and MAPK Pathways
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- mitogen-activated protein kinase, p38α, ERK2, protein-protein interaction, hydrogen-deuterium exchange mass spectrometry, substrate binding, Elk-1, nucleoporins, activation loop
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Enzyme Activation, Models, Molecular, Molecular Sequence Data, Mutation, Peptides, Protein Binding, Mass Spectrometry, Sequence Alignment, Protein Structure, Tertiary, Mitogen-Activated Protein Kinases, Rats
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