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Document Type
Journal ArticlePublication Date
2007-06-08Keywords
Animals; Animals, Newborn; COS Cells; Cadherins; Cell Membrane; Cercopithecus aethiops; Dendritic Spines; Endocytosis; Hippocampus; Humans; Mice; Microscopy, Confocal; Mutation; Neuronal Plasticity; Organ Culture Techniques; Patch-Clamp Techniques; Protein Binding; Protein Transport; Rats; Receptors, N-Methyl-D-Aspartate; Synapses; Synaptic Transmission; beta CateninLife Sciences
Medicine and Health Sciences
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Show full item recordAbstract
Enduring forms of synaptic plasticity are thought to require ongoing regulation of adhesion molecules, such as N-cadherin, at synaptic junctions. Little is known about the activity-regulated trafficking of adhesion molecules. Here we demonstrate that surface N-cadherin undergoes a surprisingly high basal rate of internalization. Upon activation of NMDA receptors (NMDAR), the rate of N-cadherin endocytosis is significantly reduced, resulting in an accumulation of N-cadherin in the plasma membrane. Beta-catenin, an N-cadherin binding partner, is a primary regulator of N-cadherin endocytosis. Following NMDAR stimulation, beta-catenin accumulates in spines and exhibits increased binding to N-cadherin. Overexpression of a mutant form of beta-catenin, Y654F, prevents the NMDAR-dependent regulation of N-cadherin internalization, resulting in stabilization of surface N-cadherin molecules. Furthermore, the stabilization of surface N-cadherin blocks NMDAR-dependent synaptic plasticity. These results indicate that NMDAR activity regulates N-cadherin endocytosis, providing a mechanistic link between structural plasticity and persistent changes in synaptic efficacy.Source
Neuron. 2007 Jun 7;54(5):771-85. Link to article on publisher's siteDOI
10.1016/j.neuron.2007.05.013Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32842PubMed ID
17553425Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.neuron.2007.05.013