Cited by 202Advanced Glycation End Products researchProtein Kinase Regulation and GTPase SignalingMelanoma and MAPK Pathways

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The receptor for advanced glycation end‐products (RAGE) directly binds to ERK by a D‐domain‐like docking site

Ishihara, Katsuya, Tsutsumi, Kae, Kawane, Shiho, Nakajima, Motowo, Kasaoka, Tatsuhiko·2003·FEBS Letters

DOI 10.1016/s0014-5793(03)00846-9

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Abstract

The receptor for advanced glycation end‐products (RAGE)‐mediated cellular activation through the mitogen‐activated protein kinase (MAPK) cascade, activation of NF‐κB and Rho family small G‐proteins, cdc42/Rac, is implicated in the pathogenesis of inflammatory disorders and tumor growth/metastasis. However, the precise molecular mechanisms for the initiation of cell signaling by RAGE remain to be elucidated. In this study, proteins which directly bind to the cytoplasmic C‐terminus of RAGE were purified from rat lung extracts using an affinity chromatography technique and identified to be extracellular signal‐regulated protein kinase‐1 and ‐2 (ERK‐1/2). Their interactions were confirmed by immunoprecipitation of ERK‐1/2 from RAGE‐expressing HT1080 cell extracts with anti‐RAGE antibody. Furthermore, the augmentation of kinase activity of RAGE‐bound ERK upon the stimulation of cells with amphoterin was demonstrated by determining the phosphorylation level of myelin basic protein, an ERK substrate. In vitro binding studies using a series of C‐terminal deletion mutants of human RAGE revealed the importance of the membrane‐proximal cytoplasmic region of RAGE for the direct ERK–RAGE interaction. This region contained a sequence similar to the D‐domain, a ERK docking site which is conserved in some ERK substrates including MAPK‐interacting kinase‐1/2, mitogen‐ and stress‐activated protein kinase‐1, and ribosomal S6 kinase. These data suggest that ERK may play a role in RAGE signaling through direct interaction with RAGE.

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Authors: Ishihara, K., Tsutsumi, K., Kawane, S., Nakajima, M., & Kasaoka, T.
Affiliations: Novartis (Japan) (JP)
ORCID: Nakajima, Motowo
Venue: FEBS Letters
Publisher: Wiley
Published: 2003-08-06
Volume: 550
Issue: 1-3
Pages: 107-113
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/s0014-5793(03)00846-9
OpenAlex: W1965497701
Cited by: 201
References: 47
Citations by year: 2026: 3 · 2025: 4 · 2024: 2 · 2023: 5 · 2022: 10 · 2021: 8 · 2020: 7 · 2019: 6 · 2018: 6 · 2017: 9 · 2016: 9 · 2015: 6 · 2014: 12 · 2013: 10 · 2012: 9
FWCI: 4.96
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
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
Keywords: receptor for advanced glycation end products, RAGE, ERK1/2, D domain, MAPK signaling, protein-protein interaction, myelin basic protein phosphorylation, amphoterin, RAGE signaling
MeSH terms: Receptor for Advanced Glycation End Products, Amino Acid Sequence, Animals, Binding Sites, Cell Extracts, Cells, Cultured, Cytoplasm, Myelin Basic Protein, Humans, Lung, Male, Phosphorylation, Receptors, Immunologic, Conserved Sequence, Rats, Wistar, Sequence Deletion, Protein Structure, Tertiary, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, HMGB1 Protein, Mitogen-Activated Protein Kinase 3, Mice, Rats

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The receptor for advanced glycation end‐products (RAGE) directly binds to ERK by a D‐domain‐like docking site

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