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

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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

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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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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: Kallunki, T
Su, B
Tsigelny, I
Dérijard, B
Davis, R
Karin, M
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: 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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JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation.

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