Physiological inhibitors of the catalytic subunit of cAMP-dependent protein kinase: effect of magnesium-ATP on protein-protein interactions

Diverse biochemical effects of different neurotransmitters or hormones that stimulate cAMP production may occur through activation of compartmentalized pools of cAMP-dependent protein kinase (PKA). Evidence suggests that compartmentalization of type II PKA is maintained through protein-protein interactions between the regulatory subunit and specific anchoring proteins.

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Regulation of the exocytotic machinery by cAMP-dependent protein kinase: implications for presynaptic plasticity

Biochemical Society Transactions ◽

10.1042/bst0310824 ◽

2003 ◽

Vol 31 (4) ◽

pp. 824-827 ◽

Cited By ~ 56

Author(s):

G.J.O. Evans ◽

A. Morgan

Keyword(s):

Protein Kinase ◽

Protein Interactions ◽

Cell Types ◽

Protein Protein Interactions ◽

Dependent Protein Kinase ◽

Camp Dependent Protein Kinase ◽

Cysteine String Protein ◽

Presynaptic Plasticity ◽

Dependent Protein

For over a decade, the enhancement of regulated exocytosis by cAMP-dependent protein kinase (PKA) has remained unexplained at the molecular level. The fact that this phenomenon has been observed in such a wide variety of secretory cell types, from pancreatic β-cells to neurons, suggests that it is an important and fundamental mechanism. Extensive analysis of the phosphorylation of exocytotic proteins has yielded few substrates of PKA in vitro, and fewer still have had physiological effects attributed to their phosphorylation. Here we review two proteins that do fulfil these criteria: the synaptic vesicle proteins cysteine string protein (CSP) and Snapin. Phosphorylation of these proteins by PKA produces changes in their respective protein–protein interactions, and has been attributed to modulation of the vesicle priming (Snapin) and vesicle fusion (CSP) stages of exocytosis. We also discuss how the function of CSP and Snapin phosphorylation might fit into an interesting aspect of the PKA-dependent enhancement of exocytosis: presynaptic plasticity in the brain.

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A novel bacterial vector system for monitoring protein-protein interactions in the cAMP-dependent protein kinase complex

Gene ◽

10.1016/s0378-1119(96)00601-4 ◽

1997 ◽

Vol 185 (1) ◽

pp. 5-9 ◽

Cited By ~ 6

Author(s):

Michael T Cairns ◽

Andrew J Green ◽

Patricia M White ◽

Patrick G Johnston ◽

Sydney Brenner

Keyword(s):

Protein Kinase ◽

Protein Interactions ◽

Vector System ◽

Protein Protein Interactions ◽

Dependent Protein Kinase ◽

Camp Dependent Protein Kinase ◽

Bacterial Vector ◽

Dependent Protein

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High-resolution crystal structure of cAMP-dependent protein kinase fromCricetulus griseus

Acta Crystallographica Section F Structural Biology Communications ◽

10.1107/s2053230x1501242x ◽

2015 ◽

Vol 71 (8) ◽

pp. 1088-1093 ◽

Cited By ~ 5

Author(s):

Denis Kudlinzki ◽

Verena L. Linhard ◽

Krishna Saxena ◽

Sridhar Sreeramulu ◽

Santosh Gande ◽

...

Keyword(s):

Protein Kinase ◽

High Resolution ◽

Protein Interactions ◽

Protein Protein Interactions ◽

Dependent Protein Kinase ◽

Cellular Processes ◽

Camp Dependent Protein Kinase ◽

Dependent Protein ◽

Functional Regulation ◽

Very High

Protein kinases (PKs) are dynamic regulators of numerous cellular processes. Their phosphorylation activity is determined by the conserved kinase core structure, which is maintained by the interaction and dynamics with associated domains or interacting proteins. The prototype enzyme for investigations to understand the activity and regulation of PKs is the catalytic subunit of cAMP-dependent protein kinase (PKAc). Major effects of functional regulation and ligand binding are driven by only minor structural modulations in protein–protein interactions. In order to resolve such minor structural differences, very high resolution structures are required. Here, the high-resolution X-ray structure of PKAc fromCricetulus griseusis reported.

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