期刊
EMBO JOURNAL
卷 28, 期 20, 页码 3244-3255出版社
WILEY
DOI: 10.1038/emboj.2009.249
关键词
cell-adhesion molecule; neuroligin; postsynaptic density; synapse; synaptogenesis
资金
- NIH [R37 MH52804-08]
- Simons Foundation
- Korea Research Foundation (MOEHRD) [KRF-2007-357C-00093]
- Human Frontier Science Program
- Life Sciences Research Foundation
- Canadian Institutes of Health Research
Postsynaptic neuroligins are thought to perform essential functions in synapse validation and synaptic transmission by binding to, and dimerizing, presynaptic alpha- and beta-neurexins. To test this hypothesis, we examined the functional effects of neuroligin-1 mutations that impair only alpha-neurexin binding, block both alpha- and beta-neurexin binding, or abolish neuroligin-1 dimerization. Abolishing alpha-neurexin binding abrogated neuroligin-induced generation of neuronal synapses onto transfected non-neuronal cells in the so-called artificial synapse-formation assay, even though beta-neurexin binding was retained. Thus, in this assay, neuroligin-1 induces apparent synapse formation by binding to presynaptic alpha-neurexins. In transfected neurons, however, neither alpha- nor beta-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 alpha-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 alpha-neurexin binding and neuroligin dimerization, but extend beyond these activities. The EMBO Journal (2009) 28, 3244-3255. doi:10.1038/emboj.2009.249; Published online 3 September 2009
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