Kinase activity is not required for alphaCaMKII-dependent presynaptic plasticity at CA3-CA1 synapses.
Using targeted mouse mutants and pharmacologic inhibition of alphaCaMKII, we demonstrate that the alphaCaMKII protein, but not its activation, autophosphorylation or its ability to phosphorylate synapsin I, is required for normal short-term presynaptic plasticity. Furthermore, alphaCaMKII regulates the number of docked vesicles independent of its ability to be activated. These results indicate that alphaCaMKII has a nonenzymatic role in short-term presynaptic plasticity at hippocampal CA3-CA1 synapses.
Department of Neuroscience, Erasmus University Medical Center, Dr. Molewaterplein 50, 3015 GE Rotterdam, The Netherlands.
Mohammad Reza
MR
Hojjati
Geeske M
GM
van Woerden
William J
WJ
Tyler
Karl Peter
KP
Giese
Alcino J
AJ
Silva
Lucas
L
Pozzo-Miller
Ype
Y
Elgersma
D000704:Analysis of Variance; D000818:Animals; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2 / Q000235:genetics / Q000502:physiology*; D004558:Electric Stimulation; D004789:Enzyme Activation / Q000235:genetics; D019706:Excitatory Postsynaptic Potentials / Q000235:genetics; D006624:Hippocampus / Q000166:cytology*; D051379:Mice; D008810:Mice, Inbred C57BL; D008822:Mice, Transgenic; D046529:Microscopy, Electron, Transmission / Q000379:methods; D016296:Mutagenesis / Q000502:physiology; D009473:Neuronal Plasticity / Q000502:physiology*; D009474:Neurons / Q000502:physiology* / Q000528:radiation effects; D018408:Patch-Clamp Techniques / Q000379:methods; D010766:Phosphorylation; D017729:Presynaptic Terminals / Q000502:physiology* / Q000648:ultrastructure; D013569:Synapses / Q000502:physiology* / Q000648:ultrastructure; D016704:Synapsins / Q000378:metabolism; D009435:Synaptic Transmission / Q000235:genetics / Q000502:physiology*; D013572:Synaptic Vesicles / Q000502:physiology
D016704:Synapsins; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2