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Activation of the EGF Receptor by Ligand Binding and Oncogenic Mutations: The “Rotation Model”
https://oist.repo.nii.ac.jp/records/260
https://oist.repo.nii.ac.jp/records/260b07f5bb9-1b8b-41c7-997d-490b274ae43f
名前 / ファイル | ライセンス | アクション |
---|---|---|
cells-06-00013-v2 (1.5 MB)
|
Creative Commons Attribution 4.0 International
(http://creativecommons.org/licenses/by/4.0/) |
Item type | 学術雑誌論文 / Journal Article(1) | |||||
---|---|---|---|---|---|---|
公開日 | 2018-01-22 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Activation of the EGF Receptor by Ligand Binding and Oncogenic Mutations: The “Rotation Model” | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者(英) |
Purba, Endang
× Purba, Endang× Saita, Ei-ichiro× Maruyama, Ichiro |
|||||
書誌情報 |
en : Cells 巻 6, 号 2, p. 13, 発行日 2017-06-02 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | The epidermal growth factor receptor (EGFR) plays vital roles in cellular processes including cell proliferation, survival, motility, and differentiation. The dysregulated activation of the receptor is often implicated in human cancers. EGFR is synthesized as a single-pass transmembrane protein, which consists of an extracellular ligand-binding domain and an intracellular kinase domain separated by a single transmembrane domain. The receptor is activated by a variety of polypeptide ligands such as epidermal growth factor and transforming growth factor α. It has long been thought that EGFR is activated by ligand-induced dimerization of the receptor monomer, which brings intracellular kinase domains into close proximity for trans-autophosphorylation. An increasing number of diverse studies, however, demonstrate that EGFR is present as a pre-formed, yet inactive, dimer prior to ligand binding. Furthermore, recent progress in structural studies has provided insight into conformational changes during the activation of a pre-formed EGFR dimer. Upon ligand binding to the extracellular domain of EGFR, its transmembrane domains rotate or twist parallel to the plane of the cell membrane, resulting in the reorientation of the intracellular kinase domain dimer from a symmetric inactive configuration to an asymmetric active form (the “rotation model”). This model is also able to explain how oncogenic mutations activate the receptor in the absence of the ligand, without assuming that the mutations induce receptor dimerization. In this review, we discuss the mechanisms underlying the ligand-induced activation of the preformed EGFR dimer, as well as how oncogenic mutations constitutively activate the receptor dimer, based on the rotation model. | |||||
出版者 | ||||||
出版者 | MDPI | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 2073-4409 | |||||
PubMed番号 | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/28574446 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.3390/cells6020013 | |||||
権利 | ||||||
権利情報 | © 2017 The Authors. | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | http://www.mdpi.com/2073-4409/6/2/13 | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 |