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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2006-7-31
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pubmed:abstractText |
Autophosphorylation of alpha-Ca2+/calmodulin kinase II (alphaCaMKII) at Thr286 is thought to be a general effector mechanism for sustaining transcription-independent long-term potentiation (LTP) at pathways where LTP is NMDA receptor-dependent. We have compared LTP at two such hippocampal pathways in mutant mice with a disabling point mutation at the Thr286 autophosphorylation site. We find that autophosphorylation of alphaCaMKII is essential for induction of LTP at Schaffer commissural-CA1 synapses in vivo, but is not required for LTP that can be sustained over days at medial perforant path-granule cell synapses in awake mice. At these latter synapses LTP is supported by cyclic AMP-dependent signalling in the absence of alphaCaMKII signalling. Thus, the autophosphorylation of alphaCaMKII is not a general requirement for NMDA receptor-dependent LTP in the adult mouse.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16728448-10027297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16728448-10377374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16728448-10454359,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16728448-9655394
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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 |
Aug
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pubmed:issn |
0022-3751
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pubmed:author |
pubmed-author:AnwylRogerR,
pubmed-author:BlissTimothy V PTV,
pubmed-author:BradshawKarl DKD,
pubmed-author:CookeSam FSF,
pubmed-author:ErringtonMichaelM,
pubmed-author:GieseK PeterKP,
pubmed-author:HiranoAyumiA,
pubmed-author:PetersMarcoM,
pubmed-author:PlattnerFlorianF,
pubmed-author:RowanMichaelM,
pubmed-author:WuJianqunJ
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
574
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
805-18
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16728448-Action Potentials,
pubmed-meshheading:16728448-Amino Acid Substitution,
pubmed-meshheading:16728448-Animals,
pubmed-meshheading:16728448-Calcium-Calmodulin-Dependent Protein Kinase Kinase,
pubmed-meshheading:16728448-Cells, Cultured,
pubmed-meshheading:16728448-Hippocampus,
pubmed-meshheading:16728448-Long-Term Potentiation,
pubmed-meshheading:16728448-Mice,
pubmed-meshheading:16728448-Mice, Inbred C57BL,
pubmed-meshheading:16728448-Mutagenesis, Site-Directed,
pubmed-meshheading:16728448-Phosphorylation,
pubmed-meshheading:16728448-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16728448-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:16728448-Signal Transduction
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pubmed:year |
2006
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