scholarly journals G-protein-coupled receptor 30/adenylyl cyclase/protein kinase A pathway is involved in estradiol 17ß-d-glucuronide-induced cholestasis

Hepatology ◽  
2014 ◽  
Vol 59 (3) ◽  
pp. 1016-1029 ◽  
Author(s):  
Andrés E. Zucchetti ◽  
Ismael R. Barosso ◽  
Andrea C. Boaglio ◽  
Cecilia L. Basiglio ◽  
Gisel Miszczuk ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Adenylyl Cyclase ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled ◽  
Kinase A

scholarly journals Protein Kinase A-mediated Phosphorylation of the Gα13Switch I Region Alters the Gαβγ13-G Protein-coupled Receptor Complex and Inhibits Rho Activation

2002 ◽  
Vol 278 (1) ◽  
pp. 124-130 ◽  
Author(s):  
Jeanne M. Manganello ◽  
Jin-Sheng Huang ◽  
Tohru Kozasa ◽  
Tatyana A. Voyno-Yasenetskaya ◽  
Guy C. Le Breton
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
G Protein ◽  
Receptor Complex ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled ◽  
Kinase A

scholarly journals The G Protein-coupled Receptor Gpr1 and the Gα Protein Gpa2 Act through the cAMP-Protein Kinase A Pathway to Induce Morphogenesis inCandida albicans

2005 ◽  
Vol 16 (4) ◽  
pp. 1971-1986 ◽  
Author(s):  
Mykola M. Maidan ◽  
Larissa De Rop ◽  
Joke Serneels ◽  
Simone Exler ◽  
Steffen Rupp ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
G Protein ◽  
Mitogen Activated Protein Kinase ◽  
Camp Signaling ◽  
G Protein Coupled Receptor ◽  
Gene Encoding ◽  
Pka Pathway ◽  
G Protein Coupled ◽  
Kinase A

We investigated the role in cell morphogenesis and pathogenicity of the Candida albicans GPR1 gene, encoding the G protein-coupled receptor Gpr1. Deletion of C. albicans GPR1 has only minor effects in liquid hypha-inducing media but results in strong defects in the yeast-to-hypha transition on solid hypha-inducing media. Addition of cAMP, expression of a constitutively active allele of the Gα protein Gpa2 or of the catalytic protein kinase A subunit TPK1 restores the wild-type phenotype of the CaGPR1-deleted strain. Overexpression of HST7, encoding a component of the mitogen-activated protein kinase pathway, does not suppress the defect in filamentation. These results indicate that CaGpr1 functions upstream in the cAMP–protein kinase A (PKA) pathway. We also show that, in the presence of glucose, CaGpr1 is important for amino acid-induced transition from yeast to hyphal cells. Finally, as opposed to previous reports, we show that CaGpa2 acts downstream of CaGpr1 as activator of the cAMP–PKA pathway but that deletion of neither CaGpr1 nor CaGpa2 affects glucose-induced cAMP signaling. In contrast, the latter is abolished in strains lacking CaCdc25 or CaRas1, suggesting that the CaCdc25-CaRas1 rather than the CaGpr1-CaGpa2 module mediates glucose-induced cAMP signaling in C. albicans.

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