Cited by 359HER2/EGFR in Cancer ResearchProtein Kinase Regulation and GTPase SignalingLung Cancer Treatments and Mutations

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Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface

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Zhang, Xuewu, Pickin, Kerry A., Bose, Ron, Jura, Natalia, Cole, Philip A., Kuriyan, John·2007·Nature

DOI 10.1038/nature05998PMC PMC3561764

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Abstract

Members of the epidermal growth factor receptor family (EGFR/ERBB1, ERBB2/HER2, ERBB3/HER3 and ERBB4/HER4) are key targets for inhibition in cancer therapy. Critical for activation is the formation of an asymmetric dimer by the intracellular kinase domains, in which the carboxy-terminal lobe (C lobe) of one kinase domain induces an active conformation in the other. The cytoplasmic protein MIG6 (mitogen-induced gene 6; also known as ERRFI1) interacts with and inhibits the kinase domains of EGFR and ERBB2 (refs 3–5). Crystal structures of complexes between the EGFR kinase domain and a fragment of MIG6 show that a ∼25-residue epitope (segment 1) from MIG6 binds to the distal surface of the C lobe of the kinase domain. Biochemical and cell-based analyses confirm that this interaction contributes to EGFR inhibition by blocking the formation of the activating dimer interface. A longer MIG6 peptide that is extended C terminal to segment 1 has increased potency as an inhibitor of the activated EGFR kinase domain, while retaining a critical dependence on segment 1. We show that signalling by EGFR molecules that contain constitutively active kinase domains still requires formation of the asymmetric dimer, underscoring the importance of dimer interface blockage in MIG6-mediated inhibition.

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Authors: Zhang, X., Pickin, K. A., Bose, R., Jura, N., Cole, P. A., & Kuriyan, J.
Affiliations: Howard Hughes Medical Institute (US)
Johns Hopkins University (US)
Corresponding author: Kuriyan, John
ORCID: Zhang, Xuewu
Bose, Ron
Jura, Natalia
Cole, Philip A.
Kuriyan, John
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2007-11-29
Volume: 450
Issue: 7170
Pages: 741-744
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature05998
PMC: PMC3561764
OpenAlex: W2046151919
Semantic Scholar: 84bdab56e088c2422419e9cd91b3387be8d1ee60
Cited by: 357
References: 22
Citations by year: 2026: 17 · 2025: 8 · 2024: 6 · 2023: 13 · 2022: 13 · 2021: 13 · 2020: 16 · 2019: 10 · 2018: 15 · 2017: 20 · 2016: 33 · 2015: 31 · 2014: 37 · 2013: 18 · 2012: 20
FWCI: 10.09
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: Susan G. Komen for the Cure
Susan G. Komen
National Institutes of Health
National Cancer Institute (R01CA096504)
Topics: Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
Keywords: epidermal growth factor receptor, MIG6, ERBB2, HER2, allosteric inhibition, EGFR signaling, constitutively active kinase, product inhibition
MeSH terms: Animals, Binding Sites, Chlorocebus aethiops, Humans, Models, Biological, Models, Molecular, Phosphorylation, Protein Binding, Protein Structure, Tertiary, Crystallography, X-Ray, Dimerization, COS Cells, Tumor Suppressor Proteins, Adaptor Proteins, Signal Transducing, ErbB Receptors

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Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface

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