EGFR in Limbo
Open accessAbstract
The epidermal growth factor receptor (EGFR) is normally activated by ligand-induced dimerization. Oncogenic mutations in EGFR promote activation in a largely ligand-independent manner. Shan et al. uncover a partially disordered state of EGFR kinase, providing evidence that oncogenic mutations counteract this intrinsic structural instability to promote dimerization and aberrant activation.
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Oncogenic mutations that stabilize the juxtamembrane region cause EGFR to be constitutively active.
“Furthermore, oncogenic mutations that stabilize the juxtamembrane region cause EGFR to be constitutively active [287].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [287]
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References 10 · Cited by 5
- Authors
- Eck, M. J., & Hahn, W. C.
- Affiliations
- Harvard University (US)
- Broad Institute (US)
- Corresponding author
- Eck, Michael J.
- Hahn, William C.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 149
- Issue
- 4
- Pages
- 735-737
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2065375249
- Cited by
- 5
- References
- 10
- Citations by year
- 2022: 1 · 2021: 2 · 2019: 1 · 2017: 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA116020)
- 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, oncogenic mutations, ligand-independent receptor activation, receptor dimerization, protein structural instability, receptor tyrosine kinase
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