Abstract
Decreased expression levels of EPHB6, a member of the receptor tyrosine kinases (RTKs), are associated with an increased risk of metastasis development in early stage non-small cell lung cancer (NSCLC). However, the signaling properties of the kinase-defective EPHB6 receptor are not well-understood. Here, we show that expression of EPHB6 in A549 lung adenocarcinoma cells led to phosphorylation of the MAP kinase ERK. Conversely, siRNA based knockdown of EPHB6 reversed ERK phosphorylation. Intriguingly, EPHB6-induced phosphorylation of ERK was uncoupled by activation of the Elk-1 transcriptional factor. These analyses suggest that kinase defective EPHB6 can lead to MAPK activation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenocarcinoma / enzymology*
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Adenocarcinoma / genetics
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Cell Line, Tumor
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Enzyme Activation
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Extracellular Signal-Regulated MAP Kinases / metabolism
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Humans
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Lung Neoplasms / enzymology*
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Lung Neoplasms / genetics
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MAP Kinase Signaling System*
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Phosphorylation
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RNA Interference
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Receptor Protein-Tyrosine Kinases / genetics
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Receptor Protein-Tyrosine Kinases / metabolism*
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Receptors, Eph Family
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Time Factors
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Transfection
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ets-Domain Protein Elk-1 / metabolism
Substances
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ELK1 protein, human
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ets-Domain Protein Elk-1
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EPHB6 protein, human
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Receptor Protein-Tyrosine Kinases
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Receptors, Eph Family
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Extracellular Signal-Regulated MAP Kinases