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

2015 ◽  
Vol 71 (8) ◽  
pp. 1088-1093 ◽  
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.

Subcellular Localization of the Type II cAMP-Dependent Protein Kinase

Physiology ◽  
1992 ◽  
Vol 7 (4) ◽  
pp. 143-148 ◽  
Author(s):  
JD Scott ◽  
DW Carr
Keyword(s):  
Protein Kinase ◽  
Protein Interactions ◽  
Regulatory Subunit ◽  
Type Ii ◽  
Protein Protein Interactions ◽  
Dependent Protein Kinase ◽  
Biochemical Effects ◽  
Camp Dependent Protein Kinase ◽  
Anchoring Proteins ◽  
Dependent Protein

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.

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

2003 ◽  
Vol 31 (4) ◽  
pp. 824-827 ◽  
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.

scholarly journals Effects of Single-Nucleotide Polymorphisms in Calmodulin-Dependent Protein Kinase Kinase 2 (CAMKK2): A Comprehensive Study

2020 ◽  
Vol 2020 ◽  
pp. 1-9
Author(s):  
Zoya Khalid ◽  
Omar Almaghrabi
Keyword(s):  
Protein Kinase ◽  
Protein Interactions ◽  
Bipolar Disorders ◽  
Docking Studies ◽  
Nucleotide Polymorphisms ◽  
Protein Protein Interactions ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Healthy Activity ◽  
Protein Kinase Kinase

Calmodulin-dependent protein kinase kinase 2 (CAMKK2) is a protein kinase that belongs to the serine/threonine kinase family. It phosphorylates kinases like CAMK1, CAMK2, and AMP, and this signaling cascade is involved in various biological processes including cell proliferation, apoptosis, and proliferation. Also, the CAMKK2 signaling activity is required for the healthy activity of the brain which otherwise can cause diseases like bipolar disorders and anxiety. The current study is based on in silico bioinformatics analysis that combines sequence- and structure-based predictions to mark a SNP as damaging or neutral. The combined results from sequence-based, evolutionary conservation-based, and consensus-based tools have predicted a total of 18 nsSNPs as deleterious, and these nsSNPs were further subjected to structure-based analysis. The six mutant models of V195A, V249M, R311C, F366Y, P389T, and W445C showed a higher deviation from the wildtype protein model and hence were further taken for docking studies. The molecular docking analysis has predicted that these mutations will also be disruptive to the protein-protein interactions between CAMKK2 and PRKAG1 which will create an evident reduction in the kinase activity. The current study has enlightened us that a few of the significant mutations are prime candidates in CAMKK2 which could be the fundamental cause of various bipolar and psychiatric disorders. This is the first detailed study that predicts the deleterious nsSNPs in CAMKK2 and contributes positively in providing a better understanding of disease mechanisms.

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