Endogenous dephosphorylation of synaptosomal calmodulin-dependent protein kinase type II.
Calmodulin-dependent protein kinase Type II autophosphorylation in synaptosomes is localized to the cytoskeleton (synaptic junction), while a potent dephosphorylating activity is present in the lipid bilayer. The dephosphorylating activity is operative in intact synaptosomes and in a reconstitution system comprised of the cytoskeletal and Triton X-100 - soluble fractions. Dephosphorylation is inhibited by EDTA and pyrophosphate, but not by EGTA or NaF. The present characterization of endogenous synaptosomal dephosphorylating activity completes the regulatory cycle operating on this enzyme in which phosphorylation of calmodulin-dependent protein kinase type II inhibits its response to Ca+2 and calmodulin.
D002118:Calcium / Q000502:physiology; D003902:Detergents; D066298:In Vitro Techniques; D009419:Nerve Tissue Proteins / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D012995:Solubility; D013574:Synaptosomes / Q000201:enzymology*
D003902:Detergents; D009419:Nerve Tissue Proteins; D011494:Protein Kinases; D010744:Phosphoric Monoester Hydrolases; D002118:Calcium