Epidermal growth factor and angiotensin II regulation of extracellular signal-regulated protein kinase in rat liver epithelial WB cells

1999 ◽  
Vol 57 (4) ◽  
pp. 425-432 ◽  
Author(s):  
Li-Jun Yang ◽  
Yan-Lin Guo ◽  
Oxana Trygankova ◽  
Qiu-Yang Li ◽  
Judith A. Maloney ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Growth Factor ◽  
Protein Kinase ◽  
Epidermal Growth Factor ◽  
Rat Liver ◽  
Extracellular Signal ◽  
Epidermal Growth

scholarly journals GIT1 Functions as a Scaffold for MEK1-Extracellular Signal-Regulated Kinase 1 and 2 Activation by Angiotensin II and Epidermal Growth Factor

2004 ◽  
Vol 24 (2) ◽  
pp. 875-885 ◽  
Author(s):  
Guoyong Yin ◽  
Judith Haendeler ◽  
Chen Yan ◽  
Bradford C. Berk
Keyword(s):  
Angiotensin Ii ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Coiled Coil ◽  
Mitogen Activated Protein Kinase ◽  
Interacting Protein ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Upstream Kinase ◽  
Epidermal Growth

ABSTRACT Activation of the mitogen-activated protein kinase pathway represented by extracellular signal-regulated kinases (ERK1/2) and activation of the upstream kinase (MEK1) are critical events for growth factor signal transduction. c-Src has been proposed as a common mediator for these signals in response to both G protein-coupled receptors (GPCRs) and tyrosine kinase-coupled receptors (TKRs). Here we show that the GPCR kinase-interacting protein 1 (GIT1) is a substrate for c-Src that associates with MEK1 in vascular smooth-muscle cells and human embryonic kidney 293 cells. GIT1 binding via coiled-coil domains and a Spa2 homology domain is required for sustained activation of MEK1-ERK1/2 after stimulation with angiotensin II and epidermal growth factor. We propose that GIT1 serves as a scaffold protein to facilitate c-Src-dependent activation of MEK1-ERK1/2 in response to both GPCRs and TKRs.

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