Cited by 220Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

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Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity

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Barr, Renae K., Kendrick, Tulene S., Bogoyevitch, Marie A.·2002·Journal of Biological Chemistry

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Abstract

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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Authors: Barr, R. K., Kendrick, T. S., & Bogoyevitch, M. A.
Affiliations: The University of Western Australia (AU)
Corresponding author: Bogoyevitch, Marie A.
ORCID: Barr, Renae K.
Kendrick, Tulene S.
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)
DOI: 10.1074/jbc.m107565200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6800 d)
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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Identification of the Critical Features of a Small Peptide Inhibitor of JNK Activity

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