Dynamin II function is required for EGF-mediated Stat3 activation but not Erk1/2 phosphorylation

Growth Factors
Rodney B LuworHong-Jian Zhu

Abstract

Signalling from receptor tyrosine kinases is elicited by ligand binding which initiates the activation of many downstream signalling cascades. Endocytosis has been widely accepted as one mechanism in which cells inactivate signalling by internalising and subsequently degrading activated receptors. However, it is now evident that endocytosis of signalling receptors is important in initiation and sustaining downstream signalling. We and others have previously shown that epidermal growth factor receptor (EGFR) overexpression and activation of signal transducer and activator of transcription 3 (Stat3) are associated with tumourigenicity. Here, we examine the role of endocytosis in EGFR signal attenuation and differential signalling. Inhibition of dynamin II (Dyn II), a GTPase required for endocytosis, with a small molecular weight inhibitor, led to reduced EGF-mediated Stat3 phosphorylation and transcriptional activity in the A431 and HN5 human tumour cell lines. However, Dyn II inhibition had minimal effect on EGF-mediated EGFR and Erk1/2 phosphorylation, which is often regarded responsible for the tumourigenic function of the EGFR. Interestingly, this effect on Stat3 activation was not due to reduced EGFR/Stat3 association. Likew...Continue Reading

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Citations

Jan 25, 2013·International Journal of Molecular Sciences·Brian P Ceresa
Jan 24, 2013·The Journal of Biological Chemistry·Morgane GourlaouenAndrew R Reynolds
Sep 27, 2014·Growth Factors·Stine Louise Jeppe KnudsenLene Melsæther Grøvdal
Feb 22, 2013·Traffic·Łukasz SadowskiMarta Miaczynska
Sep 27, 2021·Experimental Hematology·Cedric S TremblayDavid J Curtis

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