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JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation.
Open accessAbstract
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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“Almost 20 years ago, it was discovered that MAPKs contain a docking site in the C-terminal lobe that binds a conserved 13-16 amino acid sequence known as the D-or KIM-motif (kinase interaction motif).”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [19]
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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)
- 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
- 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
- bronze
- doi.org
- 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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