[HTML][HTML] Translocation of autophosphorylated calcium/calmodulin-dependent protein kinase II to the postsynaptic density
Calcium/calmodulin-dependent protein kinase II (CaMKII) undergoes calcium-dependent
autophosphorylation, generating a calcium-independent form that may serve as a molecular
substrate for memory. Here we show that calcium-independent CaMKII specifically binds to
isolated postsynaptic densities (PSDs), leading to enhanced phosphorylation of many PSD
proteins including the α-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA)-type
glutamate receptor. Furthermore, binding to PSDs changes CaMKII from a substrate for …
autophosphorylation, generating a calcium-independent form that may serve as a molecular
substrate for memory. Here we show that calcium-independent CaMKII specifically binds to
isolated postsynaptic densities (PSDs), leading to enhanced phosphorylation of many PSD
proteins including the α-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA)-type
glutamate receptor. Furthermore, binding to PSDs changes CaMKII from a substrate for …