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学科主题基础医学
Functional analysis of receptor tyrosine kinase mutations in lung cancer identifies oncogenic extracellular domain mutations of ERBB2
Greulich, Heidi1,3,5,6; Kaplan, Bethany1,6; Mertins, Philipp6; Chen, Tzu-Hsiu6; Tanaka, Kumiko E.1,6; Yun, Cai-Hong7; Zhang, Xiaohong1; Lee, Se-Hoon1; Cho, Jeonghee1; Ambrogio, Lauren6; Liao, Rachel1,6; Imielinski, Marcin1,6; Banerji, Shantanu1,6; Berger, Alice H.1,6; Lawrence, Michael S.6; Zhang, Jinghui8,9; Pho, Nam H.1,6; Walker, Sarah R.1; Winckler, Wendy6; Getz, Gad6; Frank, David1; Hahn, William C.1,2,3,6; Eck, Michael J.; Mani, D. R.6; Jaffe, Jacob D.6; Carr, Steven A.6; Wong, Kwok-Kin1,3,5; Meyerson, Matthew1,2,4,6
关键词HER2 breast cancer bladder cancer
刊名PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
2012-09-04
DOI10.1073/pnas.1203201109
109期:36页:14476-14481
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Multidisciplinary Sciences
研究领域[WOS]Science & Technology - Other Topics
关键词[WOS]GROWTH-FACTOR RECEPTOR-3 ; BREAST-CANCER ; NEU ONCOGENE ; ACTIVATING MUTATIONS ; SOMATIC MUTATIONS ; INHIBITOR HKI-272 ; POINT MUTATION ; GEFITINIB ; CELLS ; PHOSPHATASE
英文摘要

We assessed somatic alleles of six receptor tyrosine kinase genes mutated in lung adenocarcinoma for oncogenic activity. Five of these genes failed to score in transformation assays; however, novel recurring extracellular domain mutations of the receptor tyrosine kinase gene ERBB2 were potently oncogenic. These ERBB2 extracellular domain mutants were activated by two distinct mechanisms, characterized by elevated C-terminal tail phosphorylation or by covalent dimerization mediated by intermolecular disulfide bond formation. These distinct mechanisms of receptor activation converged upon tyrosine phosphorylation of cellular proteins, impacting cell motility. Survival of Ba/F3 cells transformed to IL-3 independence by the ERBB2 extracellular domain mutants was abrogated by treatment with small-molecule inhibitors of ERBB2, raising the possibility that patients harboring such mutations could benefit from ERBB2-directed therapy.

语种英语
WOS记录号WOS:000308912600042
Citation statistics
Cited Times:115[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/54762
Collection北京大学基础医学院_生物物理学系
作者单位1.Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA
2.Brigham & Womens Hosp, Dept Med, Boston, MA 02115 USA
3.Brigham & Womens Hosp, Dept Pathol, Boston, MA 02115 USA
4.Dana Farber Canc Inst, Dept Med Oncol, Boston, MA 02115 USA
5.Dana Farber Canc Inst, Ctr Canc Genome Discovery, Boston, MA 02115 USA
6.Broad Inst Harvard & MIT, Cambridge, MA 02142 USA
7.Peking Univ, Hlth Sci Ctr, Dept Biophys, Beijing 100191, Peoples R China
8.St Jude Childrens Res Hosp, Dept Biotechnol, Memphis, TN 38105 USA
9.St Jude Childrens Res Hosp, Dept Computat Biol, Memphis, TN 38105 USA
Recommended Citation
GB/T 7714
Greulich, Heidi,Kaplan, Bethany,Mertins, Philipp,et al. Functional analysis of receptor tyrosine kinase mutations in lung cancer identifies oncogenic extracellular domain mutations of ERBB2[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2012,109(36):14476-14481.
APA Greulich, Heidi.,Kaplan, Bethany.,Mertins, Philipp.,Chen, Tzu-Hsiu.,Tanaka, Kumiko E..,...&Meyerson, Matthew.(2012).Functional analysis of receptor tyrosine kinase mutations in lung cancer identifies oncogenic extracellular domain mutations of ERBB2.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,109(36),14476-14481.
MLA Greulich, Heidi,et al."Functional analysis of receptor tyrosine kinase mutations in lung cancer identifies oncogenic extracellular domain mutations of ERBB2".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 109.36(2012):14476-14481.
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