Predicted structures of the cGMP binding domains of the cGMP-dependent protein kinase: a key alanine/threonine difference in evolutionary divergence of cAMP and cGMP binding sites

Biochemistry ◽  
1989 ◽  
Vol 28 (14) ◽  
pp. 6122-6127 ◽  
Author(s):  
Irene T. Weber ◽  
John B. Shabb ◽  
Jackie D. Corbin
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Binding Sites ◽  
Evolutionary Divergence ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Binding Domains ◽  
Dependent Protein ◽  
Camp And Cgmp ◽  
Kinase A

Cross-activation: overriding cAMP/cGMP selectivities of protein kinases in tissues

1992 ◽  
Vol 70 (12) ◽  
pp. 1283-1289 ◽  
Author(s):  
Hang Jiang ◽  
John B. Shabb ◽  
Jackie D. Corbin
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Cyclic Nucleotide ◽  
The Other ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Binding Domains ◽  
Dependent Protein ◽  
Camp And Cgmp

cAMP- and cGMP-dependent protein kinases are homologous proteins and are predicted to exhibit very similar three-dimensional structures. Their cyclic nucleotide binding domains share a high degree of amino acid sequence identity. cAMP- and cGMP-dependent protein kinases are activated relatively specifically by cAMP and cGMP, respectively; and a single alanine–threonine difference between cAMP- and cGMP-binding domains partially accounts for this specificity. Thus, it would be expected that cAMP and cGMP mediate separate physiological effects. However, owing in part to the lack of absolute specificity of either enzyme and to the relatively high level of cAMP or cGMP in certain tissues, it is also possible that either cyclic nucleotide could cross-activate the other kinase. Increases in either cAMP or cGMP cause pig coronary artery relaxation. However, only cGMP-dependent protein kinase specific cyclic nucleotide analogues are very effective in causing relaxation, and cAMP elevation in arteries treated with isoproterenol or forskolin activates cGMP-dependent protein kinase, in addition to cAMP-dependent protein kinase. Conversely, increases in either cAMP or cGMP cause Cl− secretion in T-84 colon carcinoma cells, and the cGMP level in T-84 cells can be elevated sufficiently by bacterial enterotoxin to activate cAMP-dependent protein kinase. These results imply specific regulation of cAMP- and cGMP-dependent protein kinases by the respective cyclic nucleotides, but either cyclic nucleotide is able to cross-activate the other kinase in certain tissues.Key words: cGMP, cAMP, smooth muscle relaxation, protein phosphorylation.

cGMP-dependent protein kinase, a chimeric protein homologous with two separate protein families

Biochemistry ◽  
1984 ◽  
Vol 23 (18) ◽  
pp. 4207-4218 ◽  
Author(s):  
Koji Takio ◽  
Roger D. Wade ◽  
Stephen B. Smith ◽  
Edwin G. Krebs ◽  
Kenneth A. Walsh ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Chimeric Protein ◽  
Protein Families ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Separate Protein ◽  
Kinase A

scholarly journals Activation of cGMP-dependent protein kinase Iα and cAMP-dependent protein kinase A isoforms by cyclic nucleotides

2011 ◽  
Vol 11 (S1) ◽  
Author(s):  
Sabine Wolter ◽  
Marina Golombek ◽  
Andreas Hammerschmidt ◽  
Frank Schwede ◽  
Hans-Gottfried Genieser ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Cyclic Nucleotides ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Kinase A
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