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dc.contributor.authorTai, Chin-Yin
dc.contributor.authorMysore, Shreesh P.
dc.contributor.authorChiu, Cindy
dc.contributor.authorSchuman, Erin M.
dc.date2022-08-11T08:08:51.000
dc.date.accessioned2022-08-23T16:10:02Z
dc.date.available2022-08-23T16:10:02Z
dc.date.issued2007-06-08
dc.date.submitted2009-02-19
dc.identifier.citationNeuron. 2007 Jun 7;54(5):771-85. <a href="http://dx.doi.org/10.1016/j.neuron.2007.05.013">Link to article on publisher's site</a>
dc.identifier.issn0896-6273 (Print)
dc.identifier.doi10.1016/j.neuron.2007.05.013
dc.identifier.pmid17553425
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32842
dc.description.abstractEnduring 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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=17553425&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.neuron.2007.05.013
dc.subjectAnimals; 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 Catenin
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleActivity-regulated N-cadherin endocytosis
dc.typeJournal Article
dc.source.journaltitleNeuron
dc.source.volume54
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1398
dc.identifier.contextkey727651
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/1398
dc.contributor.departmentDivision of Biology 114-96
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages771-85


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