NDLI: Phosphotyrosine signaling analysis of site-specific mutations on EGFRvIII identifies determinants governing glioblastoma cell growth

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Emergence and natural selection of drug-resistant prions

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Phosphotyrosine signaling analysis of site-specific mutations on EGFRvIII identifies determinants governing glioblastoma cell growth

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Phosphotyrosine signaling analysis of site-specific mutations on EGFRvIII identifies determinants governing glioblastoma cell growth

Content Provider	Royal Society of Chemistry (RSC)
Author	Flynn, Ryan A. Furnari, Frank B. White, Forest M. Miraldi, Emily R. Rosario, Amanda M. Del Huang, Paul H. Xu, Alexander M. Cavenee, Webster K. Kundukulam, Vibin A.
Copyright Year	2010
Abstract	To evaluate the role of individual EGFR phosphorylation sites in activating components of the cellular signaling network we have performed a mass spectrometry-based analysis of the phosphotyrosine network downstream of site-specific EGFRvIII mutants, enabling quantification of network-level effects of site-specific point mutations. Mutation at Y845, Y1068 or Y1148 resulted in diminished receptor phosphorylation, while mutation at Y1173 led to increased phosphorylation on multiple EGFRvIII residues. Altered phosphorylation at the receptor was recapitulated in downstream signaling network activation levels, with Y1173F mutation leading to increased phosphorylation throughout the network. Computational modeling of GBM cell growth as a function of network phosphorylation levels highlights the Erk pathway as crucial for regulating EGFRvIII-driven U87MG GBM cell behavior, with the unexpected finding that Erk1/2 is negatively correlated to GBM cell growth. Genetic manipulation of this pathway supports the model, demonstrating that EGFRvIII-expressing U87MG GBM cells are sensitive to Erk activation levels. Additionally, we developed a model describing glioblastoma cell growth based on a reduced set of phosphoproteins, which represent potential candidates for future development as therapeutic targets for EGFRvIII-positive glioblastoma patients.
Starting Page	1227
Ending Page	1237
Page Count	11
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	6
Issue Number	7
Journal	Molecular BioSystems
DOI	10.1039/c001196g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Phosphorylation Extracellular signal\u2013regulated kinases Cell surface receptor Mutation Glioblastoma multiforme EGFR Epidermal growth factor receptor Erk
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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ANALYSIS OF SITE-SPECIFIC MUTATIONS ON EGFRVIII PHOSPHOTYROSINE SIGNALING NETWORK IDENTIFIES DETERMINANTS GOVERNING U87MG GLIOBLASTOMA CELL GROWTH

Epidermal growth factor receptor and EGFRvIII in glioblastoma: signaling pathways and targeted therapies.

ErbB2 Stabilizes Epidermal Growth Factor Receptor (EGFR) Expression via Erk and Sprouty2 in Extracellular Matrix-detached Cells

EGFR Mutations and Signaling Pathways in Glioblastoma: Implications for Pathogenesis and Therapeutic Targeting

Epidermal to Mesenchymal Transition and Failure of EGFR-Targeted Therapy in Glioblastoma

Prognostic effect of epidermal growth factor receptor and EGFRvIII in glioblastoma multiforme patients.

Contribution of Ectodomain Mutations in Epidermal Growth Factor Receptor to Signaling in Glioblastoma Multiforme

Kinase Activator-Receiver Preference in ErbB Heterodimers Is Determined by Intracellular Regions and Is Not Coupled to Extracellular Asymmetry

Lycorine inhibits glioblastoma multiforme growth through EGFR suppression

Phosphotyrosine signaling analysis of site-specific mutations on EGFRvIII identifies determinants governing glioblastoma cell growth

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ANALYSIS OF SITE-SPECIFIC MUTATIONS ON EGFRVIII PHOSPHOTYROSINE SIGNALING NETWORK IDENTIFIES DETERMINANTS GOVERNING U87MG GLIOBLASTOMA CELL GROWTH

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