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Science 2 April 1999: Vol. 284. no. 5411, pp. 162 - 167 DOI: 10.1126/science.284.5411.162
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Reports
Dynamic Control of CaMKII Translocation and Localization in Hippocampal Neurons by NMDA Receptor Stimulation
Kang Shen,
Tobias Meyer
*
Calcium-calmodulin-dependent protein kinase II (CaMKII) is thought
to increase synaptic strength by phosphorylating
postsynaptic density (PSD) ion channels and signaling proteins. It is
shown that N-methyl-D-aspartate (NMDA) receptor
stimulation reversibly translocates green fluorescent protein-tagged
CaMKII from an F-actin-bound to a PSD-bound state. The translocation
time was controlled by the ratio of expressed -CaMKII to -CaMKII
isoforms. Although F-actin dissociation into the cytosol required
autophosphorylation of or calcium-calmodulin binding to
-CaMKII, PSD translocation required binding of calcium-calmodulin to
either the - or -CaMKII subunits. Autophosphorylation
of CaMKII indirectly prolongs its PSD localization by increasing the
calmodulin-binding affinity.
Department of Cell Biology and Department of Pharmacology and
Cancer Biology, Box 3709, Duke University Medical Center, Durham, NC
27710, USA.
*
To whom correspondence should be addressed. E-mail:
tobias{at}cellbio.duke.edu
Read the Full Text
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PNAS
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- Association of Calcium/Calmodulin-dependent Kinase II with Developmentally Regulated Splice Variants of the Postsynaptic Density Protein Densin-180.
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- Mechanism and Regulation of Calcium/Calmodulin-dependent Protein Kinase II Targeting to the NR2B Subunit of the N-Methyl-D-aspartate Receptor.
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- Activation of Ca2+/Calmodulin-dependent Protein Kinase II within Post-synaptic Dendritic Spines of Cultured Hippocampal Neurons.
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- Protein Kinase C Activation Modulates alpha -Calmodulin Kinase II Binding to NR2A Subunit of N-Methyl-D-Aspartate Receptor Complex.
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- Inositol 1,4,5-Trisphosphate 3-Kinase A Associates with F-actin and Dendritic Spines via Its N Terminus.
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PNAS
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