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The Journal of Neuroscience, March 23, 2005, 25(12):3107-3112; doi:10.1523/JNEUROSCI.0085-05.2005

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BRIEF COMMUNICATION
Visualization of Synaptic Ca²⁺ /Calmodulin-Dependent Protein Kinase II Activity in Living Neurons

Keizo Takao,^1,2,3 Ken-Ichi Okamoto,¹ Terunaga Nakagawa,¹ Rachael L. Neve,⁵ Takeharu Nagai,⁴ Atsushi Miyawaki,⁴ Tsutomu Hashikawa,³ Shigeo Kobayashi,² and Yasunori Hayashi¹

¹RIKEN-Massachusetts Institute of Technology (MIT) Neuroscience Research Center, The Picower Center for Learning and Memory, Department of Brain and Cognitive Sciences, MIT, Cambridge, Massachusetts 02139, ²Division of Biological Information, Department of Intelligence Science and Technology, Graduate School of Informatics, Kyoto University, Kyoto 606-8501, Japan, ³Laboratory for Neural Architecture and ⁴Laboratory for Cell Function Dynamics, Advanced Technology Development Group, Brain Science Institute, RIKEN, Saitama 351-0198, Japan, and ⁵Department of Psychiatry, Harvard Medical School, MRC 223, McLean Hospital, Belmont, Massachusetts 02478

Ca²⁺/calmodulin-dependent protein kinase II (CaMKII) is highly enriched in excitatory synapses in the CNS and critically involved in synaptic plasticity, learning, and memory. However, the precise temporal and spatial regulation of CaMKII activity in living cells has not been well described, because of a lack of specific methods. We tried to address this by optically detecting the conformational change in CaMKII during activation using fluorescence resonance energy transfer (FRET). The engineered FRET probe Camui detects calmodulin binding and autophosphorylation at threonine 286 that renders the enzyme constitutively active. In combination with two-photon microscopy, we demonstrate that Camui can be used to observe temporal and spatial regulation of CaMKII activity in living neurons.

Key words: Ca²⁺/calmodulin-dependent protein kinase II; fluorescent resonance energy transfer; two-photon laser-scanning microscopy; synaptic plasticity; hippocampus; excitatory amino acid

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Received Sep 9, 2003; revised February 7, 2005; accepted February 8, 2005.

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