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rdf:type |
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lifeskim:mentions |
umls-concept:C0010531,
umls-concept:C0019564,
umls-concept:C0027882,
umls-concept:C0051318,
umls-concept:C0064219,
umls-concept:C1293132,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1624581,
umls-concept:C1709059
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pubmed:issue |
6474
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pubmed:dateCreated |
1994-5-19
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pubmed:abstractText |
Phosphorylation of molecules involved in synaptic transmission by multifunctional protein kinases modulates both pre- and post-synaptic events in the central nervous system. The positioning of kinases near their substrates may be an important part of the regulatory mechanism. The A-kinase-anchoring proteins (AKAPs; ref. 3) are known to bind the regulatory subunit of cyclic AMP-dependent protein kinase A with nanomolar affinity. Here we show that anchoring of protein kinase A by AKAPs is required for the modulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid (AMPA)/kainate channels. Intracellular perfusion of cultured hippocampal neurons with peptides derived from the conserved kinase binding region of AKAPs prevented the protein kinase A-mediated regulation of AMPA/kainate currents as well as fast excitatory synaptic currents. This effect could be overcome by adding the purified catalytic subunit of protein kinase. A control peptide lacking kinase-binding activity had no effect. To our knowledge, these results provide the first evidence that anchoring of protein kinase A is crucial in the regulation of synaptic function.
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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/A Kinase Anchor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/AKAP5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Akap5 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Kainic Acid
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
368
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
853-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8159245-A Kinase Anchor Proteins,
pubmed-meshheading:8159245-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:8159245-Animals,
pubmed-meshheading:8159245-Carrier Proteins,
pubmed-meshheading:8159245-Cells, Cultured,
pubmed-meshheading:8159245-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:8159245-Forskolin,
pubmed-meshheading:8159245-Hippocampus,
pubmed-meshheading:8159245-Humans,
pubmed-meshheading:8159245-Membrane Potentials,
pubmed-meshheading:8159245-Neurons,
pubmed-meshheading:8159245-Peptide Fragments,
pubmed-meshheading:8159245-Phosphorylation,
pubmed-meshheading:8159245-Proteins,
pubmed-meshheading:8159245-Rats,
pubmed-meshheading:8159245-Receptors, AMPA,
pubmed-meshheading:8159245-Receptors, Kainic Acid,
pubmed-meshheading:8159245-Synapses
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pubmed:year |
1994
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pubmed:articleTitle |
Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons.
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pubmed:affiliation |
Vollum Institute, Oregon Health Sciences University, Portland 97201.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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