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- Title
LTP in hippocampal neurons is associated with a CaMKII-mediated increase in GluA1 surface expression.
- Authors
Appleby, Vanessa J.; Corrêa, Sonia A. L.; Duckworth, Joshua K.; Nash, Joanne E.; Noël, Jacques; Fitzjohn, Stephen M.; Collingridge, Graham L.; Molnár, Elek
- Abstract
The use of hippocampal dissociated neuronal cultures has enabled the study of molecular changes in endogenous native proteins associated with long-term potentiation. Using immunofluorescence labelling of the active (Thr286-phosphorylated) alpha-Ca2+/calmodulin-dependent protein kinase II (CaMKII) we found that CaMKII activity was increased by transient (3×1 s) depolarisation in 18- to 21-day-old cultures but not in 9- to 11-day-old cultures. The increase in Thr286 phosphorylation of CaMKII required the activation of NMDA receptors and was greatly attenuated by the CaMKII inhibitor KN-62. We compared the effects of transient depolarisation on the surface expression of GluA1 and GluA2 subunits of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor and found a preferential recruitment of the GluA1 subunit. CaMKII inhibition prevented this NMDA receptor-dependent delivery of GluA1 to the cell surface. CaMKII activation is therefore an important factor in the activity-dependent recruitment of native GluA1 subunit-containing alpha-amino- 3-hydroxy-5-methyl-4-isoxazole propionate receptors to the cell surface of hippocampal neurons.
- Subjects
GLUTAMIC acid; IMMUNOFLUORESCENCE; CELL membranes; DRUG synergism; IMMUNOCYTOCHEMISTRY; SYNAPSES
- Publication
Journal of Neurochemistry, 2011, Vol 116, Issue 4, p530
- ISSN
0022-3042
- Publication type
Article
- DOI
10.1111/j.1471-4159.2010.07133.x