NDLI: Structure of the EGF receptor transactivation circuit integrates multiple signals with cell context

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Contents

Emergence and natural selection of drug-resistant prions

Host–virus interactions during hepatitis C virus infection: a complex and dynamic molecular biosystem

Therapeutic targeting in the silent era: advances in non-viral siRNA delivery

Viral-induced human carcinogenesis: an oxidative stress perspective

Ultrasensitive detection of antibodies using a new Tus–Ter-lock immunoPCR system

Direct evaluation of cellular internalization rates using chromogenic disulfides

Moving posttranslational modifications forward to biosynthesize the glycosylated thiopeptide nocathiacin I in Nocardia sp. ATCC202099

The functional capacity of the natural amino acids for molecular recognition

Cytokine-associated drug toxicity in human hepatocytes is associated with signaling network dysregulation

Systematic delineation of optimal cytokine concentrations to expand hematopoietic stem/progenitor cells in co-culture with mesenchymal stem cells

Complete genome sequence and comparative analysis of Shewanella violacea, a psychrophilic and piezophilic bacterium from deep sea floor sediments

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

Characterization of fullerene colloidal suspension in a cell culture medium for in vitro toxicity assessment

Beyond the bounds of orthology: functional inference from metagenomic context

Linear covariance models to examine the determinants of protein levels in Lactococcus lactis

Binding of the anticancer alkaloid sanguinarine to double stranded RNAs: Insights into the structural and energetics aspects

Transcriptional feedbacks in mammalian signal transduction pathways facilitate rapid and reliable protein induction

Quantitative determination of protein stability and ligand binding using a green fluorescent protein reporter system

Structure of the EGF receptor transactivation circuit integrates multiple signals with cell context

Signal sequence as a determinant in expressing disulfide-stabilized single chain antibody variable fragments (sc-dsFv) against human VEGF

Silicon nitride as a versatile growth substrate for microspectroscopic imaging and mapping of individual cells

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Structure of the EGF receptor transactivation circuit integrates multiple signals with cell context

Content Provider	Royal Society of Chemistry (RSC)
Author	Joslin, Elizabeth J. Bollinger, Nikki Wiley, H. Steven Lauffenburger, Douglas A. Opresko, Lee K. Shankaran, Harish
Copyright Year	2010
Abstract	Transactivation of the epidermal growth factor receptor (EGFR) is thought to be a process by which a variety of cellular inputs can be integrated into a single signaling pathway through either stimulated proteolysis (shedding) of membrane-anchored EGFR ligands or by modification of the activity of the EGFR. As a first step towards building a predictive model of the EGFR transactivation circuit, we quantitatively defined how signals from multiple agonists were integrated both upstream and downstream of the EGFR to regulate extracellular signal regulated kinase (ERK) activity in human mammary epithelial cells. By using a “non-binding” reporter of ligand shedding, we found that transactivation triggers a positive feedback loop from ERK back to the EGFR such that ligand shedding drives EGFR-stimulated ERK that in turn drives further ligand shedding. Importantly, activated Ras and ERK levels were nearly linear functions of ligand shedding and the effect of multiple, sub-saturating inputs was additive. Simulations showed that ERK-mediated feedback through ligand shedding resulted in a stable steady-state level of activated ERK, but also showed that the extracellular environment can modulate the level of feedback. Our results suggest that the transactivation circuit acts as a context-dependent integrator and amplifier of multiple extracellular signals and that signal integration can effectively occur at multiple points in the EGFR pathway.
Starting Page	1293
Ending Page	1306
Page Count	14
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	6
Issue Number	7
Journal	Molecular BioSystems
DOI	10.1039/c003921g
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Reporter gene Ras Cell surface receptor Proteolysis Kinase Ligand Mitogen-activated protein kinase Ras subfamily Transactivation EGFR Epidermal growth factor receptor Growth factor
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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Carbachol Stimulates Transactivation of Epidermal Growth Factor Receptor and Mitogen-activated Protein Kinase in T84Cells IMPLICATIONS FOR CARBACHOL-STIMULATED CHLORIDE SECRETION

Stimulation of the Mitogen-activated Protein Kinase Cascade and Tyrosine Phosphorylation of the Epidermal Growth Factor Receptor by Hepatopoietin

Src and Pyk2 Mediate G-protein-coupled Receptor Activation of Epidermal Growth Factor Receptor (EGFR) but Are Not Required for Coupling to the Mitogen-activated Protein (MAP) Kinase Signaling Cascade

Allosteric regulation of epidermal growth factor (EGF) receptor ligand binding by tyrosine kinase inhibitors

Epidermal Growth Factor Receptor Transactivation Is Required for Mitogen-Activated Protein Kinase Activation by Muscarinic Acetylcholine Receptors in HaCaT Keratinocytes

Activation of BAD by Therapeutic Inhibition of Epidermal Growth Factor Receptor and Transactivation by Insulin-like Growth Factor Receptor

STRUCTURE OF THE EGF RECEPTOR TRANSACTIVATION CIRCUIT INTEGRATES MULTIPLE SIGNALS WITH CELL CONTEXT

Thrombin-induced p38 mitogen-activated protein kinase activation is mediated by epidermal growth factor receptor transactivation pathway

Oncogenic Ha-Ras-dependent Mitogen-activated Protein Kinase Activity Requires Signaling Through the Epidermal Growth Factor Receptor

Structure of the EGF receptor transactivation circuit integrates multiple signals with cell context

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