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Cited by 821Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesMelanoma and MAPK Pathways

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

A conserved docking motif in MAP kinases common to substrates, activators and regulators

Tanoue, Takuji, Adachi, Makoto, Moriguchi, Tetsuo, Nishida, Eisuke·2000·Nature Cell Biology
DOI 10.1038/35000065
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Abstract

Mitogen-activated protein kinases (MAPKs) are specifically phosphorylated and activated by the MAPK kinases, phosphorylate various targets such as MAPK-activated protein kinases and transcription factors, and are inactivated by specific phosphatases. Recently, docking interactions via the non-catalytic regions of MAPKs have been suggested to be important in regulating these reactions. Here we identify docking sites in MAPKs and in MAPK-interacting enzymes. A docking domain in extracellular-signal-regulated kinase (ERK), a MAPK, serves as a common site for binding to the MAPK kinase MEK1, the MAPK-activated protein kinase MNK1 and the MAPK phosphatase MKP3. Two aspartic acids in this domain are essential for docking, one of which is mutated in the sevenmaker mutant of Drosophila ERK/Rolled. A corresponding domain in the MAPKs p38 and JNK/SAPK also serves as a common docking site for their MEKs, MAPK-activated protein kinases and MKPs. These docking interactions increase the efficiency of the enzymatic reactions. These findings reveal a hitherto unidentified docking motif in MAPKs that is used in common for recognition of their activators, substrates and regulators.

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Metadata

Authors
Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E.
Affiliations
Kyoto University (JP)
Corresponding author
Nishida, Eisuke
ORCID
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2000-01-17
Volume
2
Issue
2
Pages
110-116
ISSN
  • 1465-7392 (ISSN-L)
  • 1476-4679
DOI
10.1038/35000065
OpenAlex
W2083117403
Cited by
816
References
42
Citations by year
2026: 13 · 2025: 16 · 2024: 15 · 2023: 25 · 2022: 26 · 2021: 17 · 2020: 16 · 2019: 24 · 2018: 20 · 2017: 25 · 2016: 23 · 2015: 27 · 2014: 19 · 2013: 28 · 2012: 32
FWCI
19.91
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
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 › Melanoma and MAPK Pathways
Keywords
mitogen-activated protein kinase, extracellular signal-regulated kinase, MEK1, MKP-3, MAPK phosphatase, p38 MAPK, SAPK/JNK, MAPK kinase, aspartic acid residues, protein-protein interaction, kinase activation, substrate recognition
MeSH terms
Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Tyrosine Phosphatases, Conserved Sequence, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Mitogen-Activated Protein Kinase 1, Amino Acid Motifs, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, p38 Mitogen-Activated Protein Kinases, MAP Kinase Kinase 1, Dual Specificity Phosphatase 6

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