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Changes in the distribution of calcium calmodulin-dependent protein kinase II at the presynaptic bouton after depolarization.

Authors: Tao-Cheng, Jung-Hwa  Dosemeci, Ayse  Winters, Christine A  Reese, Thomas S 
Citation: Tao-Cheng JH, etal., Brain Cell Biol. 2006 Jun;35(2-3):117-24. doi: 10.1007/s11068-007-9012-5. Epub 2007 Sep 20.
Pubmed: (View Article at PubMed) PMID:17957478
DOI: Full-text: DOI:10.1007/s11068-007-9012-5

Phosphorylation of synapsin I by CaMKII has been reported to mobilize synaptic vesicles from the reserve pool. In the present study, the distributions of alpha-CaMKII and of synapsin I were compared in synaptic boutons of unstimulated and stimulated hippocampal neurons in culture by immunogold electron microscopy. CaMKII and synapsin I are located in separate domains in presynaptic terminals of unstimulated neurons. Label for alpha -CaMKII typically surrounds synaptic vesicle clusters and is absent from the inside of the cluster in control synapses. In contrast, intense labeling for synapsin I is found within the vesicle clusters. Following 2 minutes of depolarization in high K(+), synaptic vesicles decluster and CaMKII label disperses and mingles with vesicles and synapsin I. These results indicate that, under resting conditions, CaMKII has limited access to the synapsin I in synaptic vesicle clusters. The peripheral distribution of CaMKII around vesicle clusters suggests that CaMKII-mediated declustering progresses from the periphery towards the center, with the depth of penetration into the synaptic vesicle cluster depending on the duration of CaMKII activation. Depolarization also promotes a significant increase in CaMKII immunolabel near the presynaptic active zone. Activity-induced redistribution of CaMKII leaves it in a position to facilitate phosphorylation of additional presynaptic proteins regulating neurotransmitter release.

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RGD ID: 13702290
Created: 2018-07-18
Species: All species
Last Modified: 2018-07-18
Status: ACTIVE



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