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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2001-5-25
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pubmed:abstractText |
The N-methyl-d-aspartate (NMDA) receptor subunits NR2 possess extended intracellular C-terminal domains by which they can directly interact with a large number of postsynaptic density (PSD) proteins involved in synaptic clustering and signaling. We have previously shown that PSD-associated alpha-calmodulin kinase II (alphaCaMKII) binds with high affinity to the C-terminal domain of the NR2A subunit. Here, we show that residues 1412-1419 of the cytosolic tail of NR2A are critical for alphaCaMKII binding, and we identify, by site directed mutagenesis, PKC-dependent phosphorylation of NR2A(Ser(1416)) as a key mechanism in inhibiting alphaCaMKII-binding and promoting dissociation of alphaCaMKII.NR2A complex. In addition, we show that stimulation of PKC activity in hippocampal slices either with phorbol esters or with the mGluRs specific agonist trans-1-amino-1,3- cyclopentanedicarboxylic acid (t-ACPD) decreases alphaCaMKII binding to NMDA receptor complex. Thus, our data provide clues on understanding the molecular basis of a direct cross-talk between alphaCaMKII and PKC pathways in the postsynaptic compartment.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-amino-1,3-dicarboxycyclopentane,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloleucine,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/NR2A NMDA receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Neuroprotective Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7609-13
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11104776-Animals,
pubmed-meshheading:11104776-Calcium-Calmodulin-Dependent Protein Kinase Type 2,
pubmed-meshheading:11104776-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:11104776-Cloning, Molecular,
pubmed-meshheading:11104776-Cycloleucine,
pubmed-meshheading:11104776-Cytosol,
pubmed-meshheading:11104776-Enzyme Activation,
pubmed-meshheading:11104776-Glutathione Transferase,
pubmed-meshheading:11104776-Hippocampus,
pubmed-meshheading:11104776-Mutagenesis, Site-Directed,
pubmed-meshheading:11104776-Neuroprotective Agents,
pubmed-meshheading:11104776-Phosphorylation,
pubmed-meshheading:11104776-Plasmids,
pubmed-meshheading:11104776-Point Mutation,
pubmed-meshheading:11104776-Precipitin Tests,
pubmed-meshheading:11104776-Protein Binding,
pubmed-meshheading:11104776-Protein Kinase C,
pubmed-meshheading:11104776-Protein Structure, Tertiary,
pubmed-meshheading:11104776-Rats,
pubmed-meshheading:11104776-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:11104776-Recombinant Fusion Proteins,
pubmed-meshheading:11104776-Signal Transduction
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pubmed:year |
2001
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pubmed:articleTitle |
Protein kinase C activation modulates alpha-calmodulin kinase II binding to NR2A subunit of N-methyl-D-aspartate receptor complex.
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pubmed:affiliation |
Institute of Pharmacological Sciences, University of Milano, via Balzaretti 9, 20133 Milano, Italy. fabrizio.gardoni@unimi.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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