Subunits βγ of heterotrimeric G protein activate β2 isoform of phospholipase C

Nature ◽  
1992 ◽  
Vol 360 (6405) ◽  
pp. 686-689 ◽  
Author(s):  
Arieh Katz ◽  
Dianqing Wu ◽  
Melvin I. Simon
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Heterotrimeric G Protein

scholarly journals Activation of Phospholipase C-ε by Heterotrimeric G Protein βγ-Subunits

2001 ◽  
Vol 276 (51) ◽  
pp. 48257-48261 ◽  
Author(s):  
Michele R. Wing ◽  
Dayle Houston ◽  
Grant G. Kelley ◽  
Channing J. Der ◽  
David P. Siderovski ◽  
...  
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Heterotrimeric G Protein

scholarly journals Novel bimodal effects of the G-protein tissue transglutaminase on adrenoreceptor signalling

1999 ◽  
Vol 343 (3) ◽  
pp. 541-549 ◽  
Author(s):  
Jianwen ZHANG ◽  
Janusz TUCHOLSKI ◽  
Mathieu LESORT ◽  
Richard S. JOPE ◽  
Gail V. W. JOHNSON
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Tissue Transglutaminase ◽  
Human Neuroblastoma ◽  
Heterotrimeric G Protein ◽  
Expression Levels ◽  
Pi Hydrolysis ◽  
Low Expression

Tissue transglutaminase (tTG) is a novel G-protein that previous studies showed can couple ligand-bound activated α1B adrenoreceptors to phospholipase C-δ, resulting in phosphoinositide (PI) hydrolysis. In human neuroblastoma SH-SY5Y cells we found that although endogenous tTG can facilitate α1B adrenoreceptor-stimulated PI hydrolysis, its contribution is minor compared with the classical heterotrimeric G-protein Gq/11. Further, we show that the α1B adrenoreceptor recruits tTG to the membrane and that this recruitment is enhanced by agonist occupancy of the receptor. In addition, the effects of tTG on signalling are bimodal. At low expression levels, tTG enhanced α1B adrenoreceptor-stimulated PI hydrolysis, whereas at higher expression levels tTG attenuated significantly this response. These findings are the first to demonstrate that a protein can both facilitate and attenuate receptor-stimulated PI hydrolysis.

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