Cited by 440Melanoma and MAPK PathwaysProtein Kinase Regulation and GTPase SignalingProtein Tyrosine Phosphatases

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Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

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Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., Kornfeld, K.·1999·Genes & Development

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Abstract

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.

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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
Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
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

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Authors: Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K.
Affiliations: Washington University in St. Louis (US)
ORCID: Xing, H.
Muslin, A. J.
Kornfeld, K.
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 1999-01-15
Volume: 13
Issue: 2
Pages: 163-175
ISSN: 0890-9369 (ISSN-L)
DOI: 10.1101/gad.13.2.163
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

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Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

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