The T-type Calcium Channel Cav3.1 in Y79 Retinoblastoma Cells is Regulated by the Epidermal Growth Factor Receptor via the MAPK Signaling Pathway

2021 ◽  
pp. 1-10
Author(s):  
Umberto Banderali ◽  
Mohit Jain ◽  
Satbir Thakur ◽  
Aarthi Jayanthan ◽  
Darrell D. Belke ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Channel ◽  
Signaling Pathway ◽  
Growth Factor Receptor ◽  
Mapk Signaling ◽  
Mapk Signaling Pathway ◽  
Retinoblastoma Cells ◽  
Epidermal Growth

scholarly journals Calmodulin Regulates Intracellular Trafficking of Epidermal Growth Factor Receptor and the MAPK Signaling Pathway

2002 ◽  
Vol 13 (6) ◽  
pp. 2057-2068 ◽  
Author(s):  
Francesc Tebar ◽  
Priam Villalonga ◽  
Tatiana Sorkina ◽  
Neus Agell ◽  
Alexander Sorkin ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Signaling Pathway ◽  
Intracellular Trafficking ◽  
Growth Factor Receptor ◽  
Adaptor Protein ◽  
Mapk Signaling ◽  
Mapk Signaling Pathway ◽  
Epidermal Growth

The epidermal growth factor receptor (EGFR) is a member of the tyrosine kinase receptor family involved in signal transduction and the regulation of cellular proliferation and differentiation. It is also a calmodulin-binding protein. To examine the role of calmodulin in the regulation of EGFR, the effect of calmodulin antagonist, W-13, on the intracellular trafficking of EGFR and the MAPK signaling pathway was analyzed. W-13 did not alter the internalization of EGFR but inhibited its recycling and degradation, thus causing the accumulation of EGF and EGFR in enlarged early endosomal structures. In addition, we demonstrated that W-13 stimulated the tyrosine phosphorylation of EGFR and consequent recruitment of Shc adaptor protein with EGFR, presumably through inhibition of the calmodulin-dependent protein kinase II (CaM kinase II). W-13–mediated EGFR phosphorylation was blocked by metalloprotease inhibitor, BB94, indicating a possible involvement of shedding in this process. However, MAPK activity was decreased by W-13; dissection of this signaling pathway showed that W-13 specifically interferes with Raf-1 activity. These data are consistent with the regulation of EGFR by calmodulin at several steps of the receptor signaling and trafficking pathways.

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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