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- Title
Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation.
- Authors
Jaewon Ko; Chen Zhang; Arac, Demet; Boucard, Antony A.; Brunger, Axel T.; Südhof, Thomas C.
- Abstract
Postsynaptic neuroligins are thought to perform essential functions in synapse validation and synaptic transmission by binding to, and dimerizing, presynaptic α- and β-neurexins. To test this hypothesis, we examined the functional effects of neuroligin-1 mutations that impair only α-neurexin binding, block both α- and β-neurexin binding, or abolish neuroligin-1 dimerization. Abolishing α-neurexin binding abrogated neuroligin-induced generation of neuronal synapses onto transfected non-neuronal cells in the so-called artificial synapse-formation assay, even though β-neurexin binding was retained. Thus, in this assay, neuroligin-1 induces apparent synapse formation by binding to presynaptic α-neurexins. In transfected neurons, however, neither α- nor β-neurexin binding was essential for the ability of postsynaptic neuroligin-1 to dramatically increase synapse density, suggesting a neurexin-independent mechanism of synapse formation. Moreover, neuroligin-1 dimerization was not required for either the non-neuronal or the neuronal synapse-formation assay. Nevertheless, both α-neurexin binding and neuroligin-1 dimerization were essential for the increase in apparent synapse size that is induced by neuroligin-1 in transfected neurons. Thus, neuroligin-1 performs diverse synaptic functions by mechanisms that include as essential components of α-neurexin binding and neuroligin dimerization, but extend beyond these activities.
- Publication
EMBO Journal, 2009, Vol 28, Issue 20, p3244
- ISSN
0261-4189
- Publication type
Academic Journal
- DOI
10.1038/emboj.2009.249