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Journal Article

Activity-regulated N-cadherin endocytosis

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Schuman,  Erin M.
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

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Citation

Tai, C. Y., Mysore, S. P., Chiu, C., & Schuman, E. M. (2007). Activity-regulated N-cadherin endocytosis. Neuron, 54(5), 771-85. doi:10.1016/j.neuron.2007.05.013.


Cite as: https://hdl.handle.net/21.11116/0000-0007-EF40-4
Abstract
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.