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- W2808708135 abstract "Assembly, maintenance and function of synaptic junctions depend on extracellular matrix (ECM) proteins and their receptors. Here we report that Tenectin (Tnc), a Mucin-type protein with RGD motifs, is an ECM component required for the structural and functional integrity of synaptic specializations at the neuromuscular junction (NMJ) in Drosophila. Using genetics, biochemistry, electrophysiology, histology and electron microscopy, we show that Tnc is secreted from motor neurons and striated muscles and accumulates in the synaptic cleft. Tnc selectively recruits αPS2/βPS integrin at synaptic terminals, but only the cis Tnc/integrin complexes appear to be biologically active. These complexes have distinct pre- and postsynaptic functions, mediated at least in part through the local engagement of the spectrin-based membrane skeleton: the presynaptic complexes control neurotransmitter release, while postsynaptic complexes ensure the size and architectural integrity of synaptic boutons. Our study reveals an unprecedented role for integrin in the synaptic recruitment of spectrin-based membrane skeleton." @default.
- W2808708135 created "2018-06-21" @default.
- W2808708135 creator A5015195367 @default.
- W2808708135 creator A5026181704 @default.
- W2808708135 creator A5037494842 @default.
- W2808708135 creator A5042163149 @default.
- W2808708135 creator A5084741187 @default.
- W2808708135 date "2018-06-14" @default.
- W2808708135 modified "2023-09-27" @default.
- W2808708135 title "Tenectin recruits integrin to stabilize bouton architecture and regulate vesicle release at the Drosophila neuromuscular junction" @default.
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- W2808708135 doi "https://doi.org/10.7554/elife.35518" @default.
- W2808708135 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6040883" @default.