Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 32, Pages 14437-14442Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1009268107
Keywords
synaptic plasticity; structural plasticity; autophosphorylation; nonenzymatic function
Categories
Funding
- National Institutes of Health [R01 NS027337-19]
- National Institute of Neurological Disorders and Stroke-National Institutes of Health [R01 NS050944]
- Natural Science and Engineering Research Council of Canada
- Canadian Institutes of Health Research
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CaMKII is an abundant synaptic protein strongly implicated in plasticity. Overexpression of autonomous (T286D) CaMKII in CA1 hippocampal cells enhances synaptic strength if T305/T306 sites are not phosphorylated, but decreases synaptic strength if they are phosphorylated. It has generally been thought that spine size and synaptic strength covary; however, the ability of CaMKII and its various phosphorylation states to control spine size has not been previously examined. Using a unique method that allows the effects of overexpressed protein to be monitored over time, we found that all autonomous forms of CaMKII increase spine size. Thus, for instance, the T286D/T305D/T306D form increases spine size but decreases synaptic strength. Further evidence for such dissociation is provided by experiments with the T286D form that has been made catalytically dead. This form fails to enhance synaptic strength but increases spine size, presumably by a structural process. Thus very different mechanisms govern how CaMKII affects spine structure and synaptic function.
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