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- Title
Trans-synaptic adhesion between NGL-3 and LAR regulates the formation of excitatory synapses.
- Authors
Jooyeon Woo; Seok-Kyu Kwon; Seungwon Choi; Seho Kim; Jae-Ran Lee; Dunah, Anthone W.; Sheng, Morgan; Eunjoon Kim
- Abstract
Synaptic adhesion molecules regulate multiple steps of synapse formation and maturation. The great diversity of neuronal synapses predicts the presence of a large number of adhesion molecules that control synapse formation through trans-synaptic and heterophilic adhesion. We identified a previously unknown trans-synaptic interaction between netrin-G ligand–3 (NGL-3), a postsynaptic density (PSD) 95–interacting postsynaptic adhesion molecule, and leukocyte common antigen-related (LAR), a receptor protein tyrosine phosphatase. NGL-3 and LAR expressed in heterologous cells induced pre- and postsynaptic differentiation in contacting axons and dendrites of cocultured rat hippocampal neurons, respectively. Neuronal overexpression of NGL-3 increased presynaptic contacts on dendrites of transfected neurons. Direct aggregation of NGL-3 on dendrites induced coclustering of excitatory postsynaptic proteins. Knockdown of NGL-3 reduced the number and function of excitatory synapses. Competitive inhibition by soluble LAR reduced NGL-3–induced presynaptic differentiation. These results suggest that the trans-synaptic adhesion between NGL-3 and LAR regulates excitatory synapse formation in a bidirectional manner.
- Publication
Nature Neuroscience, 2009, Vol 12, Issue 4, p428
- ISSN
1097-6256
- Publication type
Academic Journal
- DOI
10.1038/nn.2279