scholarly journals Cyclic AMP-dependent protein kinase phosphorylates rabbit reticulocyte elongation factor-2 kinase and induces calcium-independent activity

1993 ◽  
Vol 293 (1) ◽  
pp. 31-34 ◽  
Author(s):  
N T Redpath ◽  
C G Proud
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Elongation Factor ◽  
Total Activity ◽  
Dependent Protein Kinase ◽  
Calcium Calmodulin Dependent ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor ◽  
Dependent Protein ◽  
Phosphopeptide Mapping

The catalytic subunit of cyclic AMP-dependent protein kinase (PKA) phosphorylated purified calcium/calmodulin-dependent eukaryotic elongation factor-2 (eEF-2) kinase, isolated from rabbit reticulocyte lysates. It maximally incorporated about 1 mol of phosphate/mol of eEF-2 kinase. The Km of eEF-2 kinase for PKA was calculated to be 7 microM. Phosphorylation of eEF-2 kinase by PKA induced calcium-independent activity which amounted to 40-50% of the total activity measured in the presence of calcium. Furthermore, the level of calcium-independent activity induced by phosphorylation by PKA was similar to that induced by the calcium-stimulated autophosphorylation of eEF-2 kinase. Phosphopeptide mapping of eEF-2 kinase labelled by autophosphorylation and by PKA revealed a number of common phosphopeptides. This suggests that PKA may phosphorylate the same site(s) which are phosphorylated autocatalytically and which are responsible for the induction of calcium-independent activity. The possible implications these findings have for the control of translation are discussed.

Virtual screening and experimental validation of eEF2K inhibitors by combining homology modeling, QSAR and molecular docking from FDA approved drugs

2019 ◽  
Vol 43 (48) ◽  
pp. 19097-19106 ◽  
Author(s):  
Wen-Ling Ye ◽  
Liu-Xia Zhang ◽  
Yi-Di Guan ◽  
Wei-Wei Xue ◽  
Alex F Chen ◽  
...  
Keyword(s):  
Experimental Validation ◽  
Elongation Factor ◽  
Dependent Protein Kinase ◽  
Calcium Calmodulin Dependent ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor ◽  
Dependent Protein ◽  
Approved Drugs ◽  
Fda Approved Drugs

Eukaryotic elongation factor-2 kinase (eEF2K), a calcium/calmodulin-dependent protein kinase, is a potential target for treating cancer.

scholarly journals Early events in the response of fast skeletal muscle to chronic low-frequency stimulation. Polyamine biosynthesis and protein phosphorylation

1982 ◽  
Vol 206 (2) ◽  
pp. 211-219 ◽  
Author(s):  
C Mastri ◽  
S Salmons ◽  
G H Thomas
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Low Frequency ◽  
Total Activity ◽  
Dependent Protein Kinase ◽  
Polyamine Biosynthesis ◽  
Cytoplasmic Proteins ◽  
Phosphorylation Pattern ◽  
Dependent Protein

The concentrations of putrescine, spermidine and spermine and the activities of ornithine decarboxylase (ODC) and S-adenosyl-L-methionine decarboxylase (SAM-D) were investigated in fast muscle subjected to chronic low-frequency electrical stimulation. Both ODC and SAM-D activities increased markedly between 18 and 48 h of stimulation. Changes in enzyme activities were followed by phasic elevations in the concentrations of putrescine, spermidine and spermine. Peak levels were reached first by putrescine at 3-4 days, followed by spermidine at about 9 days and then by spermine at about 11 days. A possible relationship was sought between these events and changes produced in vitro in the phosphorylation pattern of cytoplasmic proteins and the total activity of cyclic AMP-dependent protein kinase. However, during the early stages of stimulation, no prominent changes were seen either in the phosphorylation pattern or in the activity of cyclic AMP-dependent protein kinase. These characteristics changed significantly at a later stage (by 12 days of stimulation) and became indistinguishable from those of slow muscle by 3 to 4 weeks of stimulation.

scholarly journals Fructose 2,6-bisphosphate and 6-phosphofructo-2-kinase during liver regeneration

1990 ◽  
Vol 270 (3) ◽  
pp. 645-649 ◽  
Author(s):  
J L Rosa ◽  
F Ventura ◽  
J Carreras ◽  
R Bartrons
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Liver Regeneration ◽  
Partial Hepatectomy ◽  
Rat Liver ◽  
Total Activity ◽  
Glycogen Level ◽  
Dependent Protein Kinase ◽  
Phosphorylated Form ◽  
Dependent Protein

Glycogen and fructose 2,6-bisphosphate levels in rat liver decreased quickly after partial hepatectomy. After 7 days the glycogen level was normalized and fructose 2,6-bisphosphate concentration still remained low. The ‘active’ (non-phosphorylated) form of 6-phosphofructo-2-kinase varied in parallel with fructose 2,6-bisphosphate levels, whereas the ‘total’ activity of the enzyme decreased only after 24 h, similarly to glucokinase. The response of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from hepatectomized rats (96 h) to sn-glycerol 3-phosphate and to cyclic AMP-dependent protein kinase was different from that of the enzyme from control animals and similar to that of the foetal isoenzyme.

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