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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2007-9-7
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pubmed:abstractText |
Phosphorylation of various AMPA receptor subunits can alter synaptic transmission and plasticity at excitatory glutamatergic synapses in the central nervous system. Here, we identified threonine-840 (T840) on the GluR1 subunit of AMPA receptors as a novel phosphorylation site. T840 is phosphorylated by protein kinase C (PKC) in vitro and is a highly turned-over phosphorylation site in the hippocampus. Interestingly, the high basal phosphorylation of T840 in the hippocampus is maintained by a persistent activity of a protein kinase, which is counter-balanced by a basal protein phosphatase activity. To study the function of T840, we generated a line of mutant mice lacking this phosphorylation site using a gene knock-in technique. The mice generated lack T840, in addition to two previously identified phosphorylation sites S831 and S845. Using this mouse, we demonstrate that T840 may regulate synaptic plasticity in an age-dependent manner.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-10077673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-10364547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-10366608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-10501226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-10627585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-10856222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-10879537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-11007883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-11144359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-11163273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-11573007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-12392933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-12469130,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-12536214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-12628184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-12805550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-1350090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-14529720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-14534256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-14555717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-15163681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-15550950,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-15772359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-16846856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-3697730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-7527845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-8663994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-9197267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-9405465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-9407043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-9635194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-9856470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17689977-9856471
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1044-7431
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
86-94
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pubmed:dateRevised |
2010-10-4
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pubmed:meshHeading |
pubmed-meshheading:17689977-Animals,
pubmed-meshheading:17689977-Cell Line, Transformed,
pubmed-meshheading:17689977-Hippocampus,
pubmed-meshheading:17689977-Humans,
pubmed-meshheading:17689977-Long-Term Potentiation,
pubmed-meshheading:17689977-Male,
pubmed-meshheading:17689977-Mice,
pubmed-meshheading:17689977-Mice, Inbred C57BL,
pubmed-meshheading:17689977-Mice, Transgenic,
pubmed-meshheading:17689977-Mutation,
pubmed-meshheading:17689977-Neurons,
pubmed-meshheading:17689977-Phosphorylation,
pubmed-meshheading:17689977-Protein Kinase C,
pubmed-meshheading:17689977-Rats,
pubmed-meshheading:17689977-Rats, Sprague-Dawley,
pubmed-meshheading:17689977-Receptors, AMPA,
pubmed-meshheading:17689977-Threonine,
pubmed-meshheading:17689977-Transfection
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pubmed:year |
2007
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pubmed:articleTitle |
Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors.
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pubmed:affiliation |
Howard Hughes Medical Institute, Solomon H. Snyder Department of Neuroscience, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA. hlee21@umd.edu
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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