Fast neurotransmission requires the coordinated localization of neurotransmitter receptors opposite presynaptic release sites, which usually relies on the transsynaptic interaction of synaptic adhesion molecules. However, some extracellular proteins have been shown to coordinate pre- and postsynaptic differentiation by more elusive mechanisms. Here, we identify the nonfibrillar collagen CLE-1, a member of the evolutionarily conserved multiplexin family, as a master determinant of synapse identity in Caenorhabditis elegans . C. elegans muscle cells are innervated by both cholinergic and GABAergic motoneurons. The CLE-1B isoform is secreted by motoneurons and localizes to neuromuscular junctions. Loss of CLE-1B causes the relocalization of acetylcholine receptors to GABAergic synapses. We show that CLE-1B positions previously unidentified proteolytic fragments of the extracellular scaffold Punctin/MADD-4 to align acetylcholine receptors with cholinergic terminals and independently modulates receptor abundance. These findings reveal CLE-1 as a dual-function synaptic organizer that integrates spatial and quantitative control of postsynaptic receptor localization to maintain synapse identity.
- The nonfibrillar multiplexin collagen CLE-1 defines cholinergic synapse identity
- Melissa Cizeron - Université Claude Bernard Lyon 1Anaïs Dumas - Université Claude Bernard Lyon 1Suzanne Le Reun - Université Claude Bernard Lyon 1Laure Granger - Université Claude Bernard Lyon 1Maelle Jospin - Université Claude Bernard Lyon 1Oceane Romatif - Université Claude Bernard Lyon 1Camille Vachon - Université Claude Bernard Lyon 1Delphine Le Guern - Université Claude Bernard Lyon 1Aurore-Cecile Valfort - Université Claude Bernard Lyon 1Jean-Louis Bessereau - Mécanismes en sciences intégratives du vivant
- Science Advances , Vol.11(47)
- 99195707409311
- Université de Montpellier
- English
- Journal article
- hal-05520750