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- W2893866076 abstract "Synapse formation defines neuronal connectivity and is thus essential for neuronal circuit assembly. Trans-synaptic interactions of cell adhesion molecules are thought to induce synapse assembly. Here we demonstrate that a recently discovered and conserved short form of neurexin, γ-neurexin, which lacks canonical extracellular domains, is nonetheless sufficient to promote presynaptic assembly in the nematode C. elegans. γ- but not α-neurexin is required for assembling active zone components, recruiting synaptic vesicles, and clustering calcium channels at release sites to promote evoked synaptic transmission. Furthermore, we find that neurexin functions in parallel with the transmembrane receptor Frizzled, as the absence of both proteins leads to an enhanced phenotype-the loss of most synapses. Frizzled's pro-synaptogenic function is independent of its ligand, Wnt. Wnt binding instead eliminates synapses by inducing Frizzled's endocytosis and the downregulation of neurexin. These results reveal how pro- and anti-synaptogenic factors converge to precisely sculpt circuit formation in vivo." @default.
- W2893866076 created "2018-10-05" @default.
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- W2893866076 date "2018-10-01" @default.
- W2893866076 modified "2023-10-17" @default.
- W2893866076 title "γ-Neurexin and Frizzled Mediate Parallel Synapse Assembly Pathways Antagonized by Receptor Endocytosis" @default.
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- W2893866076 doi "https://doi.org/10.1016/j.neuron.2018.09.007" @default.
- W2893866076 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6181781" @default.
- W2893866076 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30269993" @default.
- W2893866076 hasPublicationYear "2018" @default.
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