Insulin Receptor Substrate protein 53kDa (IRSp53) is a negative regulator of myogenic differentiation

2012 ◽  
Vol 44 (6) ◽  
pp. 928-941 ◽  
Author(s):  
Ashish Misra ◽  
Bhawana George ◽  
Rajamuthiah Rajmohan ◽  
Neeraj Jain ◽  
Ming Hwa Wong ◽  
...  
2000 ◽  
Vol 14 (6) ◽  
pp. 823-836 ◽  
Author(s):  
Giorgia Razzini ◽  
Alessandra Ingrosso ◽  
Anna Brancaccio ◽  
Salvatore Sciacchitano ◽  
Diana L. Esposito ◽  
...  

2001 ◽  
Vol 309 (3) ◽  
pp. 145-148 ◽  
Author(s):  
Elizabeth A. Thomas ◽  
Pamela E. Foye ◽  
Carlos E. Alvarez ◽  
Hiroshi Usui ◽  
J. Gregor Sutcliffe

2001 ◽  
Vol 21 (12) ◽  
pp. 3947-3958 ◽  
Author(s):  
Laura Simpson ◽  
Jing Li ◽  
Danny Liaw ◽  
Ian Hennessy ◽  
Jonathan Oliner ◽  
...  

ABSTRACT PTEN is a tumor suppressor that antagonizes phosphatidylinositol-3 kinase (PI3K) by dephosphorylating the D3 position of phosphatidylinositol (3,4,5)-triphosphate (PtdIns-3,4,5-P3). Given the importance of PTEN in regulating PtdIns-3,4,5-P3 levels, we used Affymetrix GeneChip arrays to identify genes regulated by PTEN. PTEN expression rapidly reduced the activity of Akt, which was followed by a G1 arrest and eventually apoptosis. The gene encoding insulin receptor substrate 2 (IRS-2), a mediator of insulin signaling, was found to be the most induced gene at all time points. A PI3K-specific inhibitor, LY294002, also upregulated IRS-2, providing evidence that it was the suppression of the PI3K pathway that was responsible for the message upregulation. In addition, PTEN, LY294002, and rapamycin, an inhibitor of mammalian target of rapamycin, caused a reduction in the molecular weight of IRS-2 and an increase in the association of IRS-2 with PI3K. Apparently, PTEN inhibits a negative regulator of IRS-2 to upregulate the IRS-2–PI3K interaction. These studies suggest that PtdIns-3,4,5-P3 levels regulate the specific activity and amount of IRS-2 available for insulin signaling.


2015 ◽  
Vol 10 (S 01) ◽  
Author(s):  
G Dörpholz ◽  
K Ruschke ◽  
D Horbelt ◽  
G Wendel ◽  
M Poorgholi Belverdi ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document