Calcium- and calmodulin-dependent phosphorylation of AMPA type glutamate receptor subunits by endogenous protein kinases in the post-synaptic density.
We have detected immunoreactivities of AMPA receptor subunits GluR1-4 in post-synaptic density (PSD) fraction and tested whether they can be phosphorylated by endogenous kinases. Incubation of PSD with Ca2+ and calmodulin increased phosphorylation of GluR1 and GluR2/3. The phosphorylation of GluR1 was largely blocked by a Ca2+/calmodulin-dependent protein kinase type II inhibitor. Thus Ca2+/calmodulin-dependent phosphorylation of glutamate receptor may be a mechanism underlying enhanced post-synaptic receptor responsiveness in LTP.
Hayashi
Y
Y
Department of Neurophysiology, Institute for Brain Research, Faculty of Medicine, University of Tokyo, Japan.
Ishida
A
A
Katagiri
H
H
Mishina
M
M
Fujisawa
H
H
Manabe
T
T
Takahashi
T
T
D000818:Animals; D002118:Calcium / Q000502:physiology*; D002147:Calmodulin / Q000502:physiology*; D002540:Cerebral Cortex / Q000378:metabolism*; D010766:Phosphorylation; D017729:Presynaptic Terminals / Q000378:metabolism*; D011494:Protein Kinases / Q000502:physiology*; D051381:Rats; D018091:Receptors, AMPA / Q000378:metabolism*; D013997:Time Factors
D002147:Calmodulin; D018091:Receptors, AMPA; D011494:Protein Kinases; D002118:Calcium