Irreversible inactivation of diacylglycerol kinase-II requires a mediator.
Cytosolic diacylglycerol kinase was irreversibly inactivated by 5'-AMP since the enzyme remained less active after the removal of 5'-AMP by P-10 gel chromatography. The inactivation was time-dependent, suggesting the involvement of a covalent bond modification. A reconstitution experiment detected a rat brain cytosolic mediator for the effect of 5'-AMP. A protein kinase rich fraction prepared from rat liver was also capable of restoring the sensitivity of diacylglycerol kinase-II to 5'-AMP. We propose that 5'-AMP-activated protein kinase is the mediator which inactivates diacylglycerol kinase-II, possibly by phosphorylation.
Chen
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Department of Biochemistry, University of Missouri, Columbia 65212.
Klemm
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Jeng
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D000249:Adenosine Monophosphate / Q000494:pharmacology; D000818:Animals; D001921:Brain / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D019852:Diacylglycerol Kinase; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000037:antagonists & inhibitors; D007700:Kinetics; D010766:Phosphorylation; D010770:Phosphotransferases / Q000037:antagonists & inhibitors*; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats
D007527:Isoenzymes; D000249:Adenosine Monophosphate; D010770:Phosphotransferases; D011494:Protein Kinases; D019852:Diacylglycerol Kinase