Synaptic plasticity is thought to be a key process for learning, memory
and other cognitive functions of the nervous system. The initial events of
plasticity require the conversion of brief electrical signals into alterations
of the biochemical properties of synapses that last for much longer than the
initial stimuli. Here we show that a regulator of synaptic plasticity, calcium/calmodulin-dependent
protein kinase II (CaMKII), sequentially translocates to postsynaptic
sites, undergoes autophosphorylation and gets trapped for several minutes
until its dissociation is induced by secondary autophosphorylation and phosphatase
1 action. Once dissociated, CaMKII shows facilitated translocation for several
minutes. This suggests that trapping of CaMKII by its targets and priming
of CaMKII translocation may function as biochemical memory mechanisms that
change the signaling capacity of synapses.
(CaMKII), sequentially translocates to postsynaptic
sites, undergoes autophosphorylation and gets trapped for several minutes
until its dissociation is induced by secondary autophosphorylation and phosphatase
1 action. Once dissociated, CaMKII shows facilitated translocation for several
minutes. This suggests that trapping of CaMKII by its targets and priming
of CaMKII translocation may function as biochemical memory mechanisms that
change the signaling capacity of synapses.
