Heterotrimeric G-protein and signal transduction in the nematode-trapping fungus Arthrobotrys dactyloides

Planta ◽  
2001 ◽  
Vol 212 (5-6) ◽  
pp. 858-863 ◽  
Author(s):  
Tsung-Hsien Chen ◽  
Chan-San Hsu ◽  
Pui-Jen Tsai ◽  
Yi-Feng Ho ◽  
Na-Sheng Lin
Keyword(s):  
Signal Transduction ◽  
G Protein ◽  
Heterotrimeric G Protein

Signal Transduction of Heterotrimeric G Protein Goα in Glycosphingolipid Microdomains

MEMBRANE ◽  
2012 ◽  
Vol 37 (4) ◽  
pp. 168-173
Author(s):  
Toshiaki Miki ◽  
Mizuho Kaneda ◽  
Kohji Kasahara
Keyword(s):  
Signal Transduction ◽  
G Protein ◽  
Heterotrimeric G Protein

Heterotrimeric G protein Giis involved in a signal transduction pathway for ATP release from erythrocytes

2004 ◽  
Vol 286 (3) ◽  
pp. H940-H945 ◽  
Author(s):  
Jeffrey J. Olearczyk ◽  
Alan H. Stephenson ◽  
Andrew J. Lonigro ◽  
Randy S. Sprague
Keyword(s):  
Signal Transduction ◽  
G Protein ◽  
G Proteins ◽  
Pertussis Toxin ◽  
Atp Release ◽  
Signal Transduction Pathway ◽  
Protein G ◽  
Transduction Pathway ◽  
Heterotrimeric G Proteins ◽  
Heterotrimeric G Protein

Erythrocytes are reported to release ATP in response to mechanical deformation and decreased oxygen tension. Previously we proposed that receptor-mediated activation of the heterotrimeric G protein Gsresulted in ATP release from erythrocytes. Here we investigate the hypothesis that activation of heterotrimeric G proteins of the Gisubtype are also involved in a signal transduction pathway for ATP release from rabbit erythrocytes. Heterotrimeric G proteins Gαi1, Gαi2, and Gαi3but not Gαowere identified in rabbit and human erythrocyte membranes. Pretreatment of rabbit erythrocytes with pertussis toxin (100 ng/ml, 2 h), which uncouples Gi/ofrom their effector proteins, inhibited deformation-induced ATP release. Incubation of rabbit and human erythrocytes with mastoparan (Mas, 10 μM) or Mas-7 (1 μM), which are compounds that directly activate Giproteins, resulted in ATP release. However, rabbit erythrocytes did not release ATP when incubated with Mas-17 (10 μM), which is an inactive Mas analog. In separate experiments, Mas (10 μM) but not Mas-17 (10 μM) increased intracellular concentrations of cAMP when incubated with rabbit erythrocytes. Importantly, Mas-induced ATP release from rabbit erythrocytes was inhibited after treatment with pertussis toxin (100 ng/ml, 2 h). These data are consistent with the hypothesis that the heterotrimeric G protein Giis a component of a signal transduction pathway for ATP release from erythrocytes.

scholarly journals Rice dwarf mutant d1, which is defective in the alpha subunit of the heterotrimeric G protein, affects gibberellin signal transduction

2000 ◽  
Vol 97 (21) ◽  
pp. 11638-11643 ◽  
Author(s):  
M. Ueguchi-Tanaka ◽  
Y. Fujisawa ◽  
M. Kobayashi ◽  
M. Ashikari ◽  
Y. Iwasaki ◽  
...  
Keyword(s):  
Signal Transduction ◽  
G Protein ◽  
Alpha Subunit ◽  
Dwarf Mutant ◽  
Heterotrimeric G Protein
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