scholarly journals Autocrine transforming growth factor β signaling regulates extracellular signal-regulated kinase 1/2 phosphorylation via modulation of protein phosphatase 2A expression in scleroderma fibroblasts

2010 ◽  
Vol 3 (1) ◽  
pp. 25 ◽  
Author(s):  
Glady H Samuel ◽  
Andreea M Bujor ◽  
Sashidhar S Nakerakanti ◽  
Faye N Hant ◽  
Maria Trojanowska
Keyword(s):  
Growth Factor ◽  
Protein Phosphatase ◽  
Transforming Growth Factor ◽  
Protein Phosphatase 2A ◽  
Transforming Growth Factor Β ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Phosphatase 2A

scholarly journals Physical and Functional Interactions between Type I Transforming Growth Factor β Receptors and Bα, a WD-40 Repeat Subunit of Phosphatase 2A

1998 ◽  
Vol 18 (11) ◽  
pp. 6595-6604 ◽  
Author(s):  
Irene Griswold-Prenner ◽  
Craig Kamibayashi ◽  
E. Miko Maruoka ◽  
Marc C. Mumby ◽  
Rik Derynck
Keyword(s):  
Growth Factor ◽  
Protein Phosphatase ◽  
Transforming Growth Factor ◽  
Protein Phosphatase 2A ◽  
Transforming Growth Factor Β ◽  
Type I ◽  
Type Ii ◽  
Functional Interactions ◽  
Phosphatase 2A ◽  
Β Receptor

ABSTRACT We have previously shown that a WD-40 repeat protein, TRIP-1, associates with the type II transforming growth factor β (TGF-β) receptor. In this report, we show that another WD-40 repeat protein, the Bα subunit of protein phosphatase 2A, associates with the cytoplasmic domain of type I TGF-β receptors. This association depends on the kinase activity of the type I receptor, is increased by coexpression of the type II receptor, which is known to phosphorylate and activate the type I receptor, and allows the type I receptor to phosphorylate Bα. Furthermore, Bα enhances the growth inhibition activity of TGF-β in a receptor-dependent manner. Because Bα has been characterized as a regulator of phosphatase 2A activity, our observations suggest possible functional interactions between the TGF-β receptor complex and the regulation of protein phosphatase 2A.

Sign in / Sign up

Export Citation Format

Share Document