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Neuron. 2015 Aug 19;87(4):813-26. doi: 10.1016/j.neuron.2015.07.023.

A Temporary Gating of Actin Remodeling during Synaptic Plasticity Consists of the Interplay between the Kinase and Structural Functions of CaMKII.

Author information

1
Brain Science Institute, RIKEN, Wako, Saitama 351-0198, Japan.
2
Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, M5G 1X5, Canada.
3
Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Program in Molecular Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
4
RIKEN-MIT Neuroscience Research Center, The Picower Institute for Learning and Memory, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
5
Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, M5G 1X5, Canada; Department of Molecular Genetics, Faculty of Medicine, University of Toronto, Toronto, ON, M5S 1A8, Canada.
6
The Institute of Scientific and Industrial Research, Osaka University, Osaka 567-0047, Japan.
7
Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Program in Molecular Medicine, University of Maryland School of Medicine, Baltimore, MD 21201, USA; Program in Neuroscience, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
8
Brain Science Institute, RIKEN, Wako, Saitama 351-0198, Japan; RIKEN-MIT Neuroscience Research Center, The Picower Institute for Learning and Memory, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Brain and Body System Science Institute, Saitama University, Saitama 338-8570, Japan; School of Life Science, South China Normal University, Guangzhou 510631, China. Electronic address: yhayashi@brain.riken.jp.
9
Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, M5G 1X5, Canada; RIKEN-MIT Neuroscience Research Center, The Picower Institute for Learning and Memory, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Department of Molecular Genetics, Faculty of Medicine, University of Toronto, Toronto, ON, M5S 1A8, Canada. Electronic address: okamoto@lunenfeld.ca.

Erratum in

  • Neuron. 2015 Oct 21;88(2):433.

Abstract

The structural modification of dendritic spines plays a critical role in synaptic plasticity. CaMKII is a pivotal molecule involved in this process through both kinase-dependent and independent structural functions, but the respective contributions of these two functions to the synaptic plasticity remain unclear. We demonstrate that the transient interplay between the kinase and structural functions of CaMKII during the induction of synaptic plasticity temporally gates the activity-dependent modification of the actin cytoskeleton. Inactive CaMKII binds F-actin, thereby limiting access of actin-regulating proteins to F-actin and stabilizing spine structure. CaMKII-activating stimuli trigger dissociation of CaMKII from F-actin through specific autophosphorylation reactions within the F-actin binding region and permits F-actin remodeling by regulatory proteins followed by reassociation and restabilization. Blocking the autophosphorylation impairs both functional and structural plasticity without affecting kinase activity. These results underpin the importance of the interplay between the kinase and structural functions of CaMKII in defining a time window permissive for synaptic plasticity.

PMID:
26291163
PMCID:
PMC4548268
DOI:
10.1016/j.neuron.2015.07.023
[Indexed for MEDLINE]
Free PMC Article

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