scholarly journals Tyrosine Phosphorylation of the β2 Subunit of Clathrin Adaptor Complex AP-2 Reveals the Role of a Di-leucine Motif in the Epidermal Growth Factor Receptor Trafficking

2003 ◽  
Vol 278 (44) ◽  
pp. 43411-43417 ◽  
Author(s):  
Fangtian Huang ◽  
Xuejun Jiang ◽  
Alexander Sorkin
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Phosphorylation ◽  
Growth Factor Receptor ◽  
Receptor Trafficking ◽  
Epidermal Growth ◽  
Clathrin Adaptor

scholarly journals Role of Epidermal Growth Factor Receptor Signaling in the Interaction of Neisseria meningitidis with Endothelial Cells

2013 ◽  
Vol 82 (3) ◽  
pp. 1243-1255 ◽  
Author(s):  
Heiko Slanina ◽  
Sabrina Mündlein ◽  
Sabrina Hebling ◽  
Alexandra Schubert-Unkmeir
Keyword(s):  
Endothelial Cells ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Phosphorylation ◽  
Growth Factor Receptor ◽  
Content Type ◽  
Bacterial Uptake ◽  
Epidermal Growth

ABSTRACTNeisseria meningitidis, the causative agent of meningitis and septicemia, attaches to and invades various cell types. Both steps induce and/or require tyrosine phosphorylation of host cell proteins. Here, we used a phospho array platform to identify active receptor tyrosine kinases (RTKs) and key signaling nodes inN. meningitidis-infected brain endothelial cells to decipher RTK-dependent signaling pathways necessary for bacterial uptake. We detected several activated RTKs, including the ErbB family receptors epidermal growth factor receptor (EGFR), ErbB2, and ErbB4. We found that pharmacological inhibition and genetic ablation of ErbB receptor tyrosine phosphorylation and expression resulted in decreased bacterial uptake and heterologous expression of EGFR, ErbB2, or ErbB4 in Chinese ovary hamster (CHO-K1) cells, which do not express of EGFR and ErbB4; the decrease caused a significant increase in meningococcal invasion. Activation of EGFR and ErbB4 was mediated by transactivation via the common ligand HB-EGF (heparin-binding EGF-like ligand), which was significantly elevated in infected cell culture supernatants. We furthermore determined thatN. meningitidisinduced phosphorylation of EGFR at Tyr845 independent of ligand binding, which required c-Src activation and was involved in mediating uptake ofN. meningitidisinto eukaryotic cells. Increased uptake was repressed by expression of EGFR Y845F, which harbored a point mutation in the kinase domain. In addition, activation of ErbB4 at its autophosphorylation site, Tyr1284, and phosphorylation of ErbB2 Thr686 were observed. Altogether, our results provide evidence that EGFR, ErbB2, and ErbB4 are activated in response toN. meningitidisinfection and shed new light on the role of ErbB signaling in meningococcal infection biology.

scholarly journals Role of epidermal growth factor receptor degradation in gemcitabine-mediated cytotoxicity

Oncogene ◽  
2006 ◽  
Vol 26 (23) ◽  
pp. 3431-3439 ◽  
Author(s):  
F Y Feng ◽  
S Varambally ◽  
S A Tomlins ◽  
P Y Chun ◽  
C A Lopez ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Epidermal Growth

scholarly journals The p38 signaling pathway mediates quiescence of glioma stem cells by regulating epidermal growth factor receptor trafficking

Oncotarget ◽  
2017 ◽  
Vol 8 (20) ◽  
pp. 33316-33328 ◽  
Author(s):  
Akio Soeda ◽  
Justin Lathia ◽  
Brian J. Williams ◽  
Qiulian Wu ◽  
Joseph Gallagher ◽  
...  
Keyword(s):  
Stem Cells ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Signaling Pathway ◽  
Growth Factor Receptor ◽  
Receptor Trafficking ◽  
Glioma Stem Cells ◽  
Epidermal Growth
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