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N-cadherin-dependent neuron-neuron interaction is required for the maintenance of activity-induced dendrite growth.


ABSTRACT: Formation of neural circuits depends on stable contacts between neuronal processes, mediated by interaction of cell adhesion molecules, including N-cadherin. In the present study, we found that activity-dependent dendrite arborization specifically requires N-cadherin-mediated extracellular neuron-neuron interaction, because the enhancement did not occur for neurons cultured in isolation or plated on an astrocyte monolayer and was abolished by a recombinant soluble N-cadherin ectodomain. Furthermore, depolarization elevated the level of membrane-associated cadherin/catenin complexes and surface N-cadherin. Importantly, surface N-cadherin elevation is specifically required for the maintenance of nascent dendrite arbors. Through loss- and gain-of-function approaches, we showed that N-cadherin-mediated dendrite growth requires association of the cadherin/catenin complex with the actin cytoskeleton. In summary, these results identify a previously unexplored and specific function for activity-induced, N-cadherin-mediated neuron-neuron contacts in the maintenance of dendrite arbors.

SUBMITTER: Tan ZJ 

PROVIDER: S-EPMC2906874 | biostudies-other | 2010 May

REPOSITORIES: biostudies-other

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N-cadherin-dependent neuron-neuron interaction is required for the maintenance of activity-induced dendrite growth.

Tan Zhu-Jun ZJ   Peng Yun Y   Song He-Ling HL   Zheng Jing-Jing JJ   Yu Xiang X  

Proceedings of the National Academy of Sciences of the United States of America 20100510 21


Formation of neural circuits depends on stable contacts between neuronal processes, mediated by interaction of cell adhesion molecules, including N-cadherin. In the present study, we found that activity-dependent dendrite arborization specifically requires N-cadherin-mediated extracellular neuron-neuron interaction, because the enhancement did not occur for neurons cultured in isolation or plated on an astrocyte monolayer and was abolished by a recombinant soluble N-cadherin ectodomain. Furtherm  ...[more]

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