Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity
Open accessAbstract
The c-Jun N-terminal kinases (JNKs) are a subfamily of the mitogen-activated protein kinases (MAPKs). Although progress in evaluating the functions of other MAPKs has been facilitated by the characterization of specific inhibitors, no JNK-directed inhibitor is commercially available. We have identified a 21-amino acid peptide inhibitor of activated JNKs, based on amino acids 143-163 of the JNK-binding domain (JBD) of the JNK scaffolding protein, JNK-interacting protein-1 (JIP-1). This peptide, I-JIP (Inhibitor of JNK-based on JIP-1), inhibited JNK activity in vitro toward recombinant c-Jun, Elk, and ATF2 up to 90%. A truncated I-JIP (TI-JIP), the C-terminal 11 amino acids of I-JIP, directly interacted with recombinant JNKs but not its substrates as shown by surface plasmon resonance analysis. Scanning alanine replacement within truncated I-JIP identified 4 residues (Arg-156, Pro-157, Leu-160, or Leu-162) as independently critical for inhibition. JBD peptide sequences from JIP-2 and JIP-3 shared these critical residues and accordingly were effective JNK inhibitors. In contrast, peptides based on the JBDs of ATF2 and c-Jun inhibited JNK activity by <40%, which agreed with their lack of homology to the critical Arg-156 and Pro-157. These studies thus define a small peptide inhibitor sequence of JNKs based on the JIP proteins.
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The minimal JNK-binding region of JIP1 (pepJIP1) inhibits JNK activity in vitro toward c-jun, Elk, and ATF2 up to 90% with selectivity over Erk and p38.
“This peptide, pepJIP1 (a peptide version of JIP1), inhibited JNK activity in vitro toward recombinant c-jun, Elk, and ATF2 up to 90% with significant selectivity of no inhibition of the related Erk and p38 MAPKs.”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Barr et al , 2002
The binding between JNK and pepJIP1 is not dependent on the kinase activity of JNK.
“the binding between JNK and pepJIP1 is not dependent on the kinase activity of JNK (Barr et al , 2002)”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Barr et al , 2002
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- Authors
- Barr, R. K., Kendrick, T. S., & Bogoyevitch, M. A.
- Affiliations
- The University of Western Australia (AU)
- Corresponding author
- Bogoyevitch, Marie A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-03
- Volume
- 277
- Issue
- 13
- Pages
- 10987-10997
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2035262124
- Cited by
- 211
- References
- 45
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 5 · 2021: 3 · 2020: 3 · 2018: 4 · 2017: 6 · 2016: 12 · 2015: 2 · 2014: 2 · 2013: 13 · 2012: 9
- FWCI
- 4.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UWA Profiles and Research Repository (UWA) (submittedVersion)
- Funders
- National Heart Foundation of Australia
- 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 › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- JNK, c-Jun N-terminal kinase, peptide inhibitors, JIP1, MAPK inhibitors, c-Jun, elk, ATF2, critical residues, alanine scanning, protein-protein interaction, kinase inhibition
- MeSH terms
- Amino Acid Sequence, Animals, DNA-Binding Proteins, Enzyme Inhibitors, Kinetics, Molecular Sequence Data, Peptides, Phosphorylation, Proto-Oncogene Proteins, Recombinant Proteins, Substrate Specificity, Transcription Factors, Cyclic AMP Response Element-Binding Protein, Sequence Homology, Amino Acid, COS Cells, Surface Plasmon Resonance, Mitogen-Activated Protein Kinases, JNK Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases, ets-Domain Protein Elk-1, Activating Transcription Factor 2
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