The DOI matches its Crossref record; 47 of the 49 references it cites were found in a registry or an index.
Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
Open accessAbstract
MAP kinases phosphorylate specific groups of substrate proteins.Here we show that the amino acid sequence FXFP is an evolutionarily conserved docking site that mediates ERK MAP kinase binding to substrates in multiple protein families.FXFP and the D box, a different docking site, form a modular recognition system, as they can function independently or in combination.FXFP is specific for ERK, whereas the D box mediates binding to ERK and JNK MAP kinase, suggesting that the partially overlapping substrate specificities of ERK and JNK result from recognition of shared and unique docking sites.These findings enabled us to predict new ERK substrates and design peptide inhibitors of ERK that functioned in vitro and in vivo.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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 [37]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Oncogenes and signal transduction
Cantley, L. C., Auger, K. R., Carpenter, C. F., Duckworth, B. C., Graziani, A., Kapeller, R., & Soltoff, S. P. (1991) · Cell · doi:10.1016/0092-8674(91)90639-g · Cited by 2,697
The mitogen-activated protein kinase signal transduction pathway
Davis, R. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82362-6 · Cited by 2,112
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543
Regulation of transcription by MAP kinase cascades
Treisman, R. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80067-6 · Cited by 1,296
The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain
Marais, R., Wynne, J., & Treisman, R. (1993) · Cell · doi:10.1016/0092-8674(93)90237-k · Cited by 1,275
MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
Marshall, C. J. (1994) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(94)90095-7 · Cited by 1,005
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
Ternary complex factors: growth factor regulated transcriptional activators
Treisman, R. (1994) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(94)90097-3 · Cited by 676
Flagged first, then by citations
2 of the 49 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 401–440 of 440
Waas, W. F., & Dalby, K. N. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.12.004 · Cited by 3
Synaptic potentiation requires PARP1 activation: prevailing concepts are revisited
Cohen‐Armon, M., & Segal, M. (2026) · Molecular Psychiatry · doi:10.1038/s41380-025-03426-x · Cited by 2
Transforming Growth Factor Beta (TGF-β) Signaling in Head and Neck Squamous Cell Carcinoma (HNSCC)
Kudinov, A. E., & Beck, T. N. (2018) · Current cancer research · doi:10.1007/978-3-319-78762-6_4 · Cited by 2
REINFORCE-ING Chemical Language Models for Drug Discovery
Thomas, M. C., Bou, A., Gómez-Tamayo, J. C., Tresadern, G., Ahmad, M., & Fabritiis, G. D. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02053 · Cited by 3
Assaying Activation and Subcellular Localization of ERK in Cells and Tissues
Caelles, C., Bayod, C., & Morcillo, M. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6424-6_6 · Cited by 2
Protein Kinase Interactions with Regulatory and Effector Proteins
Defnet, A. E., Martinez, R., & Shapiro, P. (2020) · Springer eBooks · doi:10.1007/978-3-030-48283-1_4 · Cited by 2
Peptide‐Based Inhibitors that Target the Docking Site of ERK2
Solomon, O., Shpilt, Z., Sapir, H., Marom, S., Bibas, S., Chen, Y., Tshuva, E. Y., Yitzchaik, S., & Friedler, A. (2022) · Israel Journal of Chemistry · doi:10.1002/ijch.202200041 · Cited by 2
Discovering Functional ERK Substrates Regulating Caenorhabditis elegans Germline Development
Chen, J. J., & Arur, S. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6424-6_24 · Cited by 2
MAP Kinase Modules in Signaling
Elion, E. A. (2002) · Elsevier eBooks · doi:10.1016/b0-12-227555-1/00139-8 · Cited by 2
Functional pocketomes and complete allosteric maps of five protein kinasesPreprint
Folgado, C., Beltran, T., & Lehner, B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.04.742685 · Cited by 2
Chakraborty, A., Chakrabarty, S., Uppala, J. K., Mayer, K. A., Evans, A. J., George, J., Ghosh, C., Dey, R., Ohikhuare, F., Mirza, S. P., et al. (2026) · Communications Biology · doi:10.1038/s42003-026-10090-6 · Cited by 1
RAS and the RAF/MEK/ERK Cascade
Morrison, D. K., & Daar, I. O. (2006) · Springer eBooks · doi:10.1007/1-4020-4708-8_4 · Cited by 1
Shahid, M. N., Rasheed, S., Jamal, A., Khalid, S., & Shamim, Z. (2021) · Brazilian Archives of Biology and Technology · doi:10.1590/1678-4324-2021210169 · Cited by 1
Renin-Angiotensin System Activation and Extracellular Signal-Regulated Kinases in Glomerulonephritis
Urushihara, M., & Kinoshit, Y. (2011) · InTech eBooks · doi:10.5772/23393 · Cited by 1
MAP Kinase Modules in Signaling☆
Elion, E. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.98742-7 · Cited by 1
Basu, S., Luke, B. T., Karim, B. O., Martín, N. C. R., Lockett, S., Das, S., Andrésson, Þ., Saylor, K. L., Kozlov, S. V., Bassel, L., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.05.487175 · Cited by 1
SGEBP, a giant protein from starfish oocytes able to interact with ERK
Vergé, V., Lozano, J.-C., Schatt, P., & Peaucellier, G. (2013) · Molecular Reproduction and Development · doi:10.1002/mrd.22210
Lawler, S. E. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01530-5
EGF-Receptor Signaling in Caenorhabditis elegans Vulval Development
Moghal, N., & Sternberg, P. W. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50616-1
Davis, R. J. (2003) · Elsevier eBooks · doi:10.1016/b978-012124546-7/50545-3
Vieira, N. A. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2018.tde-25042018-143544
Herman, R. K. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.729075652.793537764
Havelange, V., & Constantinescu, S. N. (2022) · Blood · doi:10.1182/blood.2022016536
Non-canonical interactions of the Mitogen Activated Protein (MAP) kinases
Kirsch, K. P. (2021) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2021.040
Target Hyperactive ERK Signaling for Cancer Therapy
Yap, J., & Hu, J. (2023) · Springer eBooks · doi:10.1007/978-3-030-80962-1_257-1
Uppala, J. K., Chakraborty, A., George, J., Mayer, K. A., Ghosh, C., Dey, R., Chaluvally–Raghavan, P., & Dey, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.19.567283
Orand, T., Delaforge, E., Chenal, M., Tengo, M., Herrmann, T., Cortés, J., Bernadó, P., & Jensen, M. R. (2025) · Advanced Science · doi:10.1002/advs.202503987
Target Hyperactive ERK Signaling for Cancer Therapy
Yap, J., & Hu, J. (2025) · Springer eBooks · doi:10.1007/978-3-032-00771-1_257
Gomez, S. M., Homberg, L. T., Bührmann, M., Rauh, D., & Linser, R. (2026) · Angewandte Chemie · doi:10.1002/ange.202522665
Mechanistic insight into the dual phosphorylation of ERK1 and ERK2 by MEK1Preprint
Sun, Y., Peng, C., Liu, S., Zhou, F., Huang, G., Wang, J., & Hu, Q. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.13.710243
Sipieter, F. (2015) · theses.fr (ABES) · doi:10.70675/d530ded3z94aez4864z858azb556e4d75412
Control, use and misuse of cellular signalling networks
Juyoux, P. (2021) · theses.fr (ABES) · doi:10.70675/59616c42zeda8z4a8dza27fze9e6c6d83982
Zhang, Y., Pei, C.-J., Luo, Z., Zhu, Z., Wu, J., & Wang, Z. (2026) · Communications Biology · doi:10.1038/s42003-026-10502-7
Zhang, B., Xiao, Y., Liu, Y., Wang, W., Li, P., Wang, R., Jiang, C., Zhang, G., Chen, C., Sun, X., et al. (2026) · Science Advances · doi:10.1126/sciadv.adu6821
Metadata
- Authors
- Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K.
- Affiliations
- Washington University in St. Louis (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1999-01-15
- Volume
- 13
- Issue
- 2
- Pages
- 163-175
- ISSN
- 0890-9369 (ISSN-L)
- OpenAlex
- W4239714346
- Cited by
- 439
- References
- 49
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 4 · 2023: 9 · 2022: 16 · 2021: 12 · 2020: 13 · 2019: 7 · 2018: 13 · 2017: 13 · 2016: 16 · 2015: 15 · 2014: 10 · 2013: 13 · 2012: 15
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- Foundation for Barnes-Jewish Hospital
- Edward Mallinckrodt, Jr. Foundation
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- 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
- Keywords
- ERK MAP kinase, docking site, D-box, substrate specificity, JNK MAP kinase, phosphorylation, peptide inhibitors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review