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Cited by 653Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesMelanoma and MAPK Pathways

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation.

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Kallunki, 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
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Abstract

The transcriptional activity of c-Jun is augmented through phosphorylation at two sites by a c-Jun amino-terminal kinase (JNK). All cells express two distinct JNK activities, 46 and 55 kD in size. It is not clear which of them is the more important c-Jun kinase and how they specifically recognize c-Jun. The 46-kD form of JNK was identified as a new member of the MAP kinase group of signal-transducing enzymes, JNK1. Here, we report the molecular cloning of the 55-kD form of JNK, JNK2, which exhibits 83% identity and similar regulation to JNK1. Despite this close similarity, the two JNKs differ greatly in their ability to interact with c-Jun. JNK2 binds c-Jun approximately 25 times more efficiently than JNK1, and as a result has a lower Km toward c-Jun than JNK1. The structural basis for this difference was investigated and traced to a small beta-strand-like region near the catalytic pocket of the enzyme. Modeling suggests that this region is solvent exposed and therefore is likely to serve as a docking site that increases the effective concentration of c-Jun near JNK2. These results explain how two closely related MAP kinases can differ in their ability to recognize specific substrates and thereby elicit different biological responses.

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Metadata

Authors
Kallunki, T., Su, B., Tsigelny, I., Sluss, H. K., Dérijard, B., Moore, G., Davis, R., & Karin, M.
Affiliations
Howard Hughes Medical Institute (US)
ORCID
Venue
Genes & Development
Publisher
Cold Spring Harbor Laboratory
Published
1994-12-15
Volume
8
Issue
24
Pages
2996-3007
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
DOI
10.1101/gad.8.24.2996
OpenAlex
W1972145919
Cited by
642
References
34
Citations by year
2026: 7 · 2025: 5 · 2024: 4 · 2023: 3 · 2022: 2 · 2021: 3 · 2020: 6 · 2019: 2 · 2018: 8 · 2017: 8 · 2016: 7 · 2015: 6 · 2014: 15 · 2013: 15 · 2012: 21
Type
posted content
Language
en
Open access
Locations
  • Genes & Development (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Department of Energy
  • National Institutes of Health
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
JNK2, c-Jun, c-Jun N-terminal kinase, mitogen-activated protein kinase, substrate specificity, protein-protein interaction, c-Jun phosphorylation, docking site, catalytic pocket, JNK1, transcriptional activation, gene cloning
MeSH terms
Amino Acid Sequence, Binding Sites, Cell Line, Cloning, Molecular, Humans, Kinetics, Models, Molecular, Molecular Sequence Data, Molecular Weight, Protein Kinases, Transfection, Tumor Cells, Cultured, Gene Expression, Proto-Oncogene Proteins c-jun, Conserved Sequence, Sequence Homology, Amino Acid, Protein Structure, Secondary, Calcium-Calmodulin-Dependent Protein Kinases, Mitogen-Activated Protein Kinases, JNK Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase 9

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