2014年3月18日
In Vitro Reconstitution of a CaMKII Memory Switch by an NMDA Receptor-Derived Peptide
Biophysical Journal
- ,
- ,
- ,
- 巻
- 106
- 号
- 6
- 開始ページ
- 1414
- 終了ページ
- 1420
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bpj.2014.01.026
- 出版者・発行元
- Elsevier BV
Ca(2+)/Calmodulin-dependent protein kinase II (CaMKII) has been shown to play a major role in establishing memories through complex molecular interactions including phosphorylation of multiple synaptic targets. However, it is still controversial whether CaMKII itself serves as a molecular memory because of a lack of direct evidence. Here, we show that a single holoenzyme of CaMKII per se serves as an erasable molecular memory switch. We reconstituted Ca(2+)/Calmodulin-dependent CaMKII autophosphorylation in the presence of protein phosphatase 1 in vitro, and found that CaMKII phosphorylation shows a switch-like response with history dependence (hysteresis) only in the presence of an N-methyl-D-aspartate receptor-derived peptide. This hysteresis is Ca(2+) and protein phosphatase 1 concentration-dependent, indicating that the CaMKII memory switch is not simply caused by an N-methyl-D-aspartate receptor-derived peptide lock of CaMKII in an active conformation. Mutation of a phosphorylation site of the peptide shifted the Ca(2+) range of hysteresis. These functions may be crucial for induction and maintenance of long-term synaptic plasticity at hippocampal synapses.
- リンク情報
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- DOI
- https://doi.org/10.1016/j.bpj.2014.01.026
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/24655517
- PubMed Central
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985500
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000333226900024&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1016/j.bpj.2014.01.026
- ISSN : 0006-3495
- eISSN : 1542-0086
- PubMed ID : 24655517
- PubMed Central 記事ID : PMC3985500
- Web of Science ID : WOS:000333226900024