The Full-Length, Cytoplasmic C-Terminus of the β2-Adrenergic Receptor Expressed in E. coli Acts as a Substrate for Phosphorylation by Protein Kinase A, Insulin Receptor Tyrosine Kinase, GRK2, but Not Protein Kinase C and Suppresses Desensitization when Expressed in Vivo

2000 ◽  
Vol 20 (3) ◽  
pp. 451-461 ◽  
Author(s):  
Sergey Doronin ◽  
Fubao Lin ◽  
Hsien-yu Wang ◽  
Craig C. Malbon

Diabetes ◽  
1991 ◽  
Vol 40 (11) ◽  
pp. 1440-1448 ◽  
Author(s):  
H. K. Muller ◽  
M. Kellerer ◽  
B. Ermel ◽  
A. Muhlhofer ◽  
B. Obermaier-Kusser ◽  
...  


Cell ◽  
1991 ◽  
Vol 67 (4) ◽  
pp. 723-730 ◽  
Author(s):  
Takashi Okamoto ◽  
Yoshitake Murayama ◽  
Yujiro Hayashi ◽  
Masaki Inagaki ◽  
Etsuro Ogata ◽  
...  


FEBS Letters ◽  
2002 ◽  
Vol 532 (1-2) ◽  
pp. 52-56 ◽  
Author(s):  
Régine Hepp ◽  
Jean-Pierre Cabaniols ◽  
Paul A Roche


2004 ◽  
Vol 121 (2) ◽  
pp. 282
Author(s):  
S.A. Akhter ◽  
K.M. D’souza ◽  
W.H. Merrill


2002 ◽  
Vol 13 (11) ◽  
pp. 3943-3954 ◽  
Author(s):  
Elena Shumay ◽  
Xiaosong Song ◽  
Hsien-yu Wang ◽  
Craig C. Malbon

Insulin stimulates a rapid phosphorylation and sequestration of the β2-adrenergic receptor. Analysis of the signaling downstream of the insulin receptor with enzyme inhibitors revealed roles for both phosphatidylinositol 3-kinase and pp60Src. Inhibition of Src with PP2, like the inhibition of phosphatidylinositol 3-kinase with LY294002 [2-(4-morpholynyl)-8-phenyl-4H-1-benzopyran-4-one], blocked the activation of Src as well as insulin-stimulated sequestration of the β2-adrenergic receptor. Depletion of Src with antisense morpholinos also suppressed insulin-stimulated receptor sequestration. Src is shown to be phosphorylated/activated in response to insulin in human epidermoid carcinoma A431 cells as well as in mouse 3T3-L1 adipocytes and their derivative 3T3-F422A cells, well-known models of insulin signaling. Inhibition of Src with PP2 blocks the ability of insulin to sequester β2-adrenergic receptors and the translocation of the GLUT4 glucose transporters. Insulin stimulates Src to associate with the β2-adrenergic receptor/AKAP250/protein kinase A/protein kinase C signaling complex. We report a novel positioning of Src, mediating signals from insulin to phosphatidylinositol 3-kinase and to β2-adrenergic receptor trafficking.



2000 ◽  
Vol 275 (51) ◽  
pp. 40635-40640 ◽  
Author(s):  
Ming Zheng ◽  
Sheng-Jun Zhang ◽  
Wei-Zhong Zhu ◽  
Bruce Ziman ◽  
Brian K. Kobilka ◽  
...  


Diabetes ◽  
1991 ◽  
Vol 40 (11) ◽  
pp. 1440-1448 ◽  
Author(s):  
H. K. Muller ◽  
M. Kellerer ◽  
B. Ermel ◽  
A. Muhlhofer ◽  
B. Obermaier-Kusser ◽  
...  


Nature ◽  
10.1038/36362 ◽  
1997 ◽  
Vol 390 (6655) ◽  
pp. 88-91 ◽  
Author(s):  
Yehia Daaka ◽  
Louis M. Luttrell ◽  
Robert J. Lefkowitz




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