RELATIONSHIP BETWEEN cAMP-DEPENDENT PROTEIN KINASE ACTIVATION AND Ca UPTAKE INCREASE OF SARCOPLASMIC RETICULUM FRACTION OF PIG BILE DUCTS TO TETRAGASTRIN

Abstracts ◽  
1978 ◽  
pp. 32
Author(s):  
M. Kimura ◽  
I. Kimura ◽  
S. Kobayashi
Keyword(s):  
Protein Kinase ◽  
Sarcoplasmic Reticulum ◽  
Bile Ducts ◽  
Dependent Protein Kinase ◽  
Kinase Activation ◽  
Camp Dependent Protein Kinase ◽  
Protein Kinase Activation ◽  
Ca Uptake ◽  
Dependent Protein

scholarly journals Characterization of cAMP-dependent protein kinase activation by CCK in rat pancreas

FEBS Letters ◽  
1993 ◽  
Vol 316 (1) ◽  
pp. 48-52 ◽  
Author(s):  
Christopher R. Marino ◽  
Steven D. Leach ◽  
Jean F. Schaefer ◽  
Laurence J. Miller ◽  
Fred S. Gorelick
Keyword(s):  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Kinase Activation ◽  
Rat Pancreas ◽  
Camp Dependent Protein Kinase ◽  
Protein Kinase Activation ◽  
Dependent Protein

scholarly journals The type III inositol 1,4,5-trisphosphate receptor is phosphorylated by cAMP-dependent protein kinase at three sites

2005 ◽  
Vol 392 (3) ◽  
pp. 493-497 ◽  
Author(s):  
Matthew D. Soulsby ◽  
Richard J. H. Wojcikiewicz
Keyword(s):  
Protein Kinase ◽  
Ip3 Receptor ◽  
Dependent Protein Kinase ◽  
Kinase Activation ◽  
Type Iii ◽  
Camp Dependent Protein Kinase ◽  
Protein Kinase Activation ◽  
Inositol 1,4,5 Trisphosphate ◽  
Functional Consequences ◽  
Dependent Protein

IP3 (inositol 1,4,5-trisphosphate) receptors form tetrameric, IP3-gated Ca2+ channels in endoplasmic reticulum membranes, and are substrates for several kinases, including PKA (cAMP-dependent protein kinase). Activation of PKA has been reported to either enhance or inhibit type III IP3 receptor Ca2+-channel activity, but, as yet, the sites of phosphorylation remain unknown. Here, we reveal that PKA phosphorylates the type III IP3 receptor at Ser916, Ser934 and Ser1832, and that, intriguingly, each site is located close to a putative surface-exposed peptide loop. Furthermore, we demonstrate that Ser934 is considerably more susceptible to PKA-dependent phoshorylation than either Ser916 or Ser1832. These findings define the sites at which the type III IP3 receptor is phosphorylated by PKA, and provide the basis for exploring the functional consequences of this regulatory event.

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