ArticleBiophysical journal2014
In vitro reconstitution of a CaMKII memory switch by an NMDA receptor-derived peptide.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- CaMKII: a central molecular organizer of synaptic plasticity, learning and memory.Nature reviews. Neuroscience · 2022Review
- Autoregulation of switching behavior by cellular compartment size.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Role of CaFrontiers in molecular neuroscience · 2022Review
- Dynamic bistable switches enhance robustness and accuracy of cell cycle transitions.PLoS computational biology · 2021Article
- Interactions between calmodulin and neurogranin govern the dynamics of CaMKII as a leaky integrator.PLoS computational biology · 2020Article
- A multi-state model of the CaMKII dodecamer suggests a role for calmodulin in maintenance of autophosphorylation.PLoS computational biology · 2019Article
- Reciprocal Activation within a Kinase-Effector Complex Underlying Persistence of Structural LTP.Neuron · 2019Article
- The Interaction between the Drosophila EAG Potassium Channel and the Protein Kinase CaMKII Involves an Extensive Interface at the Active Site of the Kinase.Journal of molecular biology · 2018Article
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- Analog Signaling With the "Digital" Molecular Switch CaMKII.Frontiers in computational neuroscience · 2018Article
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- Multi-phasic bi-directional chemotactic responses of the growth cone.Scientific reports · 2016Article
- Article
- Biochemical principles underlying the stable maintenance of LTP by the CaMKII/NMDAR complex.Brain research · 2015Article
- First demonstration of bistability in CaMKII, a memory-related kinase.Biophysical journal · 2014Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
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.
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