Protein and phospholipid methylation during chemotaxis in Dictyostelium discoideum and its relationship to calcium movements.
Suspensions of cyclic AMP sensitive cells of Dictyostelium discoideum responded to a cyclic AMP pulse with increased methylation of a protein of molecular weight about 120,000 and increased phospholipid demethylation. Protein methylation reached its peak 15-30 sec after cyclic AMP addition. Phospholipid demethylation reached its maximum within 2 min and basal levels were recovered in 3 min. S-Adenosyl-L-methionine is probably the methyl donor. In vitro addition of 0.25 mM and 25 microM S-adenosyl-L-methionine to sonicated D. discoideum cells inhibited ATP-dependent 45Ca2+ uptake by 70% and 25%, respectively. Based on these lines of evidence we propose that protein and phospholipid methylation are involved in D. discoideum chemotaxis probably by regulation of intracellular Ca2+ movements.
D002118:Calcium / Q000378:metabolism*; D002628:Chemoreceptor Cells / Q000502:physiology; D002633:Chemotaxis; D000242:Cyclic AMP / Q000494:pharmacology; D004023:Dictyostelium / Q000502:physiology*; D005656:Fungal Proteins / Q000378:metabolism*; D008563:Membrane Lipids / Q000378:metabolism; D008745:Methylation; D008970:Molecular Weight; D010743:Phospholipids / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000378:metabolism
D005656:Fungal Proteins; D008563:Membrane Lipids; D010743:Phospholipids; D012436:S-Adenosylmethionine; D000242:Cyclic AMP; D002118:Calcium