Inhibitory autophosphorylation of CaMKII controls PSD association, plasticity, and learning Neuron
| Autor: | Sami Ikonen, Alcino J. Silva, Karl Peter Giese, Minetta Elgersma, Ofelia M. Carvalho, Esther S. Choi, Ype Elgersma, Fedorov Nikolai |
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| Přispěvatelé: | Neurosciences |
| Rok vydání: | 2002 |
| Předmět: |
Male
Neuroscience(all) Long-Term Potentiation Presynaptic Terminals Synaptic Membranes Mice Transgenic Neurotransmission Biology Inhibitory postsynaptic potential Hippocampus Synaptic Transmission environment and public health Gene Expression Regulation Enzymologic Membrane Potentials 03 medical and health sciences Mice 0302 clinical medicine Organ Culture Techniques Ca2+/calmodulin-dependent protein kinase Animals Learning Phosphorylation Maze Learning 030304 developmental biology 0303 health sciences Kinase General Neuroscience Long-Term Synaptic Depression musculoskeletal neural and ocular physiology Autophosphorylation Long-term potentiation Electric Stimulation Cell biology enzymes and coenzymes (carbohydrates) nervous system Calcium-Calmodulin-Dependent Protein Kinases Female Calcium-Calmodulin-Dependent Protein Kinase Type 2 Neuroscience Postsynaptic density Excitatory Amino Acid Antagonists 030217 neurology & neurosurgery |
| Zdroj: | Neuron, 36(3), 493-505. Cell Press |
| ISSN: | 0896-6273 |
| DOI: | 10.1016/s0896-6273(02)01007-3 |
| Popis: | To investigate the function of the alpha calcium-calmodulin-dependent kinase II (alphaCaMKII) inhibitory autophosphorylation at threonines 305 and/or 306, we generated knockin mice that express alphaCaMKII that cannot undergo inhibitory phosphorylation. In addition, we generated mice that express the inhibited form of alphaCaMKII, which resembles the persistently phosphorylated kinase at these sites. Our data demonstrate that blocking inhibitory phosphorylation increases CaMKII in the postsynaptic density (PSD), lowers the threshold for hippocampal long-term potentiation (LTP), and results in hippocampal-dependent learning that seems more rigid and less fine-tuned. Mimicking inhibitory phosphorylation dramatically decreased the association of CaMKII with the PSD and blocked both LTP and learning. These data demonstrate that inhibitory phosphorylation has a critical role in plasticity and learning. |
| Databáze: | OpenAIRE |
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