scholarly journals Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A

2000 ◽  
Vol 97 (22) ◽  
pp. 11960-11965 ◽  
Author(s):  
X. Fang ◽  
S. X. Yu ◽  
Y. Lu ◽  
R. C. Bast ◽  
J. R. Woodgett ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Kinase A

scholarly journals Protein Kinase A Negatively Modulates the Nuclear Accumulation of NF-ATc1 by Priming for Subsequent Phosphorylation by Glycogen Synthase Kinase-3

2002 ◽  
Vol 277 (50) ◽  
pp. 48664-48676 ◽  
Author(s):  
Colleen M. Sheridan ◽  
E. Kevin Heist ◽  
Chan R. Beals ◽  
Gerald R. Crabtree ◽  
Phyllis Gardner
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Nuclear Accumulation ◽  
Glycogen Synthase Kinase 3 ◽  
Kinase A

scholarly journals FRAT1, a Substrate-specific Regulator of Glycogen Synthase Kinase-3 Activity, Is a Cellular Substrate of Protein Kinase A

2006 ◽  
Vol 281 (46) ◽  
pp. 35021-35029 ◽  
Author(s):  
Thilo Hagen ◽  
Darren A. E. Cross ◽  
Ainsley A. Culbert ◽  
Andrew West ◽  
Sheelagh Frame ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Kinase A

scholarly journals The In Vivo Activity of Ime1, the Key Transcriptional Activator of Meiosis-Specific Genes in Saccharomyces cerevisiae, Is Inhibited by the Cyclic AMP/Protein Kinase A Signal Pathway through the Glycogen Synthase Kinase 3-β Homolog Rim11

2004 ◽  
Vol 24 (16) ◽  
pp. 6967-6979 ◽  
Author(s):  
Ifat Rubin-Bejerano ◽  
Shira Sagee ◽  
Osnat Friedman ◽  
Lilach Pnueli ◽  
Yona Kassir
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinase A ◽  
Glycogen Synthase ◽  
Transcriptional Activator ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Diploid Cells ◽  
Kinase A

ABSTRACT Phosphorylation is the main mode by which signals are transmitted to key regulators of developmental pathways. The glycogen synthase kinase 3 family plays pivotal roles in the development and well-being of all eukaryotic organisms. Similarly, the budding yeast homolog Rim11 is essential for the exit of diploid cells from the cell cycle and for entry into the meiotic developmental pathway. In this report we show that in vivo, in cells grown in a medium promoting vegetative growth with acetate as the sole carbon source (SA medium), Rim11 phosphorylates Ime1, the master transcriptional activator required for entry into the meiotic cycle and for the transcription of early meiosis-specific genes. We demonstrate that in the presence of glucose, the kinase activity of Rim11 is inhibited. This inhibition could be due to phosphorylation on Ser-5, Ser-8, and/or Ser-12 because in the rim11S5AS8AS12A mutant, Ime1 is incorrectly phosphorylated in the presence of glucose and cells undergo sporulation. We further show that this nutrient signal is transmitted to Rim11 and consequently to Ime1 by the cyclic AMP/protein kinase A signal transduction pathway. Ime1 is phosphorylated in SA medium on at least two residues, Tyr-359 and Ser-302 and/or Ser-306. Ser-302 and Ser-306 are part of a consensus site for the mammalian homolog of Rim11, glycogen synthase kinase 3-β. Phosphorylation on Tyr-359 but not Ser-302 or Ser-306 is essential for the transcription of early meiosis-specific genes and sporulation. We show that Tyr-359 is phosphorylated by Rim11.

scholarly journals Convergence of 3′,5′-Cyclic Adenosine 5′-Monophosphate/Protein Kinase A and Glycogen Synthase Kinase-3β/β-Catenin Signaling in Corpus Luteum Progesterone Synthesis

Endocrinology ◽  
2009 ◽  
Vol 150 (11) ◽  
pp. 5036-5045 ◽  
Author(s):  
Lynn Roy ◽  
Claudia A. McDonald ◽  
Chao Jiang ◽  
Dulce Maroni ◽  
Anthony J. Zeleznik ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Corpus Luteum ◽  
Glycogen Synthase ◽  
Regulatory Protein ◽  
Glycogen Synthase Kinase ◽  
Proximal Promoter ◽  
Progesterone Secretion ◽  
Progesterone Synthesis ◽  
Kinase A

Progesterone secretion by the steroidogenic cells of the corpus luteum (CL) is essential for reproduction. Progesterone synthesis is under the control of LH, but the exact mechanism of this regulation is unknown. It is established that LH stimulates the LH receptor/choriogonadotropin receptor, a G-protein coupled receptor, to increase cAMP and activate cAMP-dependent protein kinase A (PKA). In the present study, we tested the hypothesis that cAMP/PKA-dependent regulation of the Wnt pathway components glycogen synthase kinase (GSK)-3β and β-catenin contributes to LH-dependent steroidogenesis in luteal cells. We observed that LH via a cAMP/PKA-dependent mechanism stimulated the phosphorylation of GSK3β at N-terminal Ser9 causing its inactivation and resulted in the accumulation of β-catenin. Overexpression of N-terminal truncated β-catenin (Δ90 β-catenin), which lacks the phosphorylation sites responsible for its destruction, significantly augmented LH-stimulated progesterone secretion. In contrast, overexpression of a constitutively active mutant of GSK3β (GSK-S9A) reduced β-catenin levels and inhibited LH-stimulated steroidogenesis. Chromatin immunoprecipitation assays demonstrated the association of β-catenin with the proximal promoter of the StAR gene, a gene that expresses the steroidogenic acute regulatory protein, which is a cholesterol transport protein that controls a rate-limiting step in steroidogenesis. Collectively these data suggest that cAMP/PKA regulation of GSK3β/β-catenin signaling may contribute to the acute increase in progesterone production in response to LH.

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