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Endothelin-1 induces p66Shc activation through EGF receptor transactivation: Role of beta(1)Pix/Galpha(i3) interaction.

Abstract：

:Endothelin-1 (ET-1) is a vasoconstrictor peptide known to be a potent mitogen for glomerular mesangial cells. We have shown that ET-1 stimulates the adaptor protein p66Shc through Rac/Cdc42 guanine nucleotide exchange factor beta(1)Pix. In this study, we demonstrate that ET-1-induced serine phosphorylation of p66Shc is mediated through Galpha(i3). Pertussis toxin treatment of cells induced a significant decrease in the interaction between beta(1)Pix and ET(A)-R, and an increase in the binding of Galpha(i3) and G(beta1) to beta(1)Pix. Activation of heterotrimeric G proteins by AlF(4)(-) resulted in an increase of Galpha(i3) binding to beta(1)Pix, which was significantly disrupted in cells expressing beta(1)Pix dimerization deficient mutant, beta(1)PixDelta (602-611). In cells expressing beta(1)PixDelta (602-611), ET-1-induced p66Shc activation was also significantly decreased. Specific inhibition of EGF receptor by AG1478 blocked ET-1-induced p66Shc activation and the binding of p66Shc and Galpha(i3) to beta(1)Pix. Inhibition of Erk1/2 blocked p66Shc activation induced by ET-1. Altogether, our results indicate that ET-1 activates p66Shc through EGF receptor transactivation, leading to the activation of Galpha(i3), beta(1)Pix and Erk1/2.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Chahdi A,Sorokin A

doi

10.1016/j.cellsig.2009.09.039

subject

Has Abstract

pub_date

2010-02-01 00:00:00

pages

325-9

issue

2

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(09)00289-7

journal_volume

22

pub_type

杂志文章

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