Neurexin mediates the assembly of presynaptic terminals

Camin Dean, Francisco G. Scholl, Jenny Choih, Shannon DeMaria, James Berger, Ehud Isacoff, Peter Scheiffele

Research output: Contribution to journalArticlepeer-review

Abstract

Neurexins are a large family of proteins that act as neuronal cell-surface receptors. The function and localization of the various neurexins, however, have not yet been clarified. Beta-neurexins are candidate receptors for neuroligin-1, a postsynaptic membrane protein that can trigger synapse formation at axon contacts. Here we report that neurexins are concentrated at synapses and that purified neuroligin is sufficient to cluster neurexin and to induce presynaptic differentiation. Oligomerization of neuroligin is required for its function, and we find that beta-neurexin clustering is sufficient to trigger the recruitment of synaptic vesicles through interactions that require the cytoplasmic domain of neurexin. We propose a two-step model in which postsynaptic neuroligin multimers initially cluster axonal neurexins. In response to this clustering, neurexins nucleate the assembly of a cytoplasmic scaffold to which the exocytotic apparatus is recruited.

Original languageEnglish (US)
Pages (from-to)708-716
Number of pages9
JournalNature neuroscience
Volume6
Issue number7
DOIs
StatePublished - Jul 1 2003
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)

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