Phosphorylation-dependent reversible translocation of Ca2+/calmodulin-dependent protein kinase II to the postsynaptic densities.
The translocation of soluble Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) to postsynaptic densities (PSDs) was investigated. When soluble CaM kinase II previously autophosphorylated was incubated with PSDs, the kinase was precipitated by centrifugation, indicating that the soluble kinase associated with PSDs and formed a PSD-CaM kinase II complex. Ca2+-independent activity generated by autophosphorylation of the kinase was retained in the complex. A number of PSD proteins were phosphorylated by the kinase associated with PSDs in both the absence and presence of Ca2+. When PSD-CaM kinase II complex was incubated at 30 degrees C, the enzyme was dephosphorylated and released from the complex. These results indicate that CaM kinase II reversibly translocates to PSDs in a phosphorylation-dependent manner.
Yamauchi
T
T
Department of Biochemistry, Faculty of Pharmaceutical Sciences, The University of Tokushima, Japan.
Yoshimura
Y
Y
D000818:Animals; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D051379:Mice; D010766:Phosphorylation; D016548:Prosencephalon / Q000201:enzymology; D051381:Rats; D013569:Synapses / Q000201:enzymology*
D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases