Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.11 (AMPK)
 12,425 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Alterations in ribosomal function were examined following phosphorylation of 40 S ribosomal subunits by the cAMP-dependent protein kinase and two cAMP-independent protein kinases, protease-activated kinases I and II. The cAMP-dependent protein kinase incorporated 2.0 mol of phosphate/mol of 40 S ribosomal subunits; ribosomal protein S6 was the sole phosphate acceptor. Phosphorylation of 40 S ribosomal subunits by the cAMP-dependent protein kinase inhibited the binding of AUG by 41% and poly(A,U,G) by 25% when compared with nonphosphorylated 40 S ribosomal subunits. In addition, phosphorylation of 40 S ribosomal subunits by the cAMP-dependent protein kinase inhibited translation of poly(A,U,G) by 30% in a reconstituted protein-synthesizing system. Protease-activated kinase II incorporated an average of 2.5 mol of phosphate/mol of 40 S ribosomal subunits which was distributed in equimolar amounts in derivatives of S6 containing one to four phosphates. Phosphorylation of 40 S ribosomal subunits by protease-activated kinase II increased the binding of AUG and poly(A,U,G) by 26 and 42%, respectively. Poly(A,U,G)-directed translation was stimulated 15% over that observed with nonphosphorylated ribosomes and 45% over that observed with ribosomes phosphorylated by the cAMP-dependent protein kinase. Protease-activated kinase I incorporated 1.0 mol of phosphate/mol of 40 S ribosomal subunits into ribosomal protein S10. Phosphorylation of 40 S ribosomal subunits by protease-activated kinase I did not alter the binding of AUG or poly(A,U,G). The effects of phosphorylation of 40 S ribosomal subunits by protease-activated kinase I on protein synthesis could not be examined due to the rapid release of phosphate from S10 in the reconstituted translation system.
 ...
PMID:Changes in ribosome function by cAMP-dependent and cAMP-independent phosphorylation of ribosomal protein S6. 664 64

Analysis of Saccharomyces cerevisiae genome revealed no sequence homologous to cyclic GMP (cGMP) dependent protein kinase from other organisms. Here we demonstrate that cyclic AMP (cAMP) dependent protein kinase purified from S. cerevisiae was almost equally activated by cAMP and cGMP in 3 x 10(-6) M concentrations of either nucleotide in the presence of Mg2+ ions. Interestingly, if Mn2+ ions were used instead of Mg2+, cGMP was only 30% as effective as cAMP in the activation of cAMP-dependent protein kinase. Analogs of cAMP such as 8-chloro-cAMP and 3':5'-cyclic monophosphate of ribofuranosylbenzimidazole were as potent as cAMP in the enzyme activation, while N6,2'-O-dibutyryl-cAMP activated the enzyme to a lower extent. It was also found that yeast cAMP-dependent protein kinase can be activated by limited proteolytic digestion. The results presented were obtained with protamine and ribosomal protein S10 used as phosphorylation substrates.
 ...
PMID:PKA from Saccharomyces cerevisiae can be activated by cyclic AMP and cyclic GMP. 1034 18