scholarly journals Regulation of single inositol 1,4,5-trisphosphate receptor channel activity by protein kinase A phosphorylation

2008 ◽  
Vol 586 (15) ◽  
pp. 3577-3596 ◽  
Author(s):  
Larry E. Wagner ◽  
Suresh K. Joseph ◽  
David I. Yule
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Channel Activity ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Kinase A ◽  
Receptor Channel

scholarly journals Protein Kinase A Increases Type-2 Inositol 1,4,5-Trisphosphate Receptor Activity by Phosphorylation of Serine 937

2009 ◽  
Vol 284 (37) ◽  
pp. 25116-25125 ◽  
Author(s):  
Matthew J. Betzenhauser ◽  
Jenna L. Fike ◽  
Larry E. Wagner ◽  
David I. Yule
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Receptor Activity ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Kinase A

scholarly journals Association of Type 1 Inositol 1,4,5-Trisphosphate Receptor with AKAP9 (Yotiao) and Protein Kinase A

2004 ◽  
Vol 279 (18) ◽  
pp. 19375-19382 ◽  
Author(s):  
Huiping Tu ◽  
Tie-Shan Tang ◽  
Zhengnan Wang ◽  
Ilya Bezprozvanny
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Kinase A

Interactions Between the Inositol 1,4,5-Trisphosphate and Cyclic AMP Signaling Pathways Regulate Larval Molting in Drosophila

Genetics ◽  
2001 ◽  
Vol 158 (1) ◽  
pp. 309-318 ◽  
Author(s):  
K Venkatesh ◽  
G Siddhartha ◽  
Rohit Joshi ◽  
Sonal Patel ◽  
Gaiti Hasan
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Signaling Pathways ◽  
Feedback Inhibition ◽  
Receptor Gene ◽  
Dominant Negative ◽  
Neural Signals ◽  
Inositol 1,4,5 Trisphosphate ◽  
Kinase A ◽  
Insp3 Receptor

Abstract Larval molting in Drosophila, as in other insects, is initiated by the coordinated release of the steroid hormone ecdysone, in response to neural signals, at precise stages during development. In this study we have analyzed, using genetic and molecular methods, the roles played by two major signaling pathways in the regulation of larval molting in Drosophila. Previous studies have shown that mutants for the inositol 1,4,5-trisphosphate receptor gene (itpr) are larval lethals. In addition they exhibit delays in molting that can be rescued by exogenous feeding of 20-hydroxyecdysone. Here we show that mutants for adenylate cyclase (rut) synergize, during larval molting, with itpr mutant alleles, indicating that both cAMP and InsP3 signaling pathways function in this process. The two pathways act in parallel to affect molting, as judged by phenotypes obtained through expression of dominant negative and dominant active forms of protein kinase A (PKA) in tissues that normally express the InsP3 receptor. Furthermore, our studies predict the existence of feedback inhibition through protein kinase A on the InsP3 receptor by increased levels of 20-hydroxyecdysone.

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