Title : Structural basis for integration of
GluD receptors within synaptic organizer complexes
Abstract :
- Ionotropic glutamate receptor ( iGluR ) family members are integrated into supramolecular complexes that modulate their location and function at excitatory synapses
- However, a lack of structural information beyond isolated receptors or fragments thereof currently limits the mechanistic understanding of physiological iGluR signaling
- Here, we report structural and functional analyses of the prototypical molecular bridge linking postsynaptic iGluR δ2 ( GluD2 ) and presynaptic β- neurexin 1 (β-NRX1) via Cbln1 , a C1q-like synaptic organizer
- We show how Cbln1 hexamers "anchor" GluD2 amino-terminal domain dimers to monomeric β-NRX1
- This arrangement promotes synaptogenesis and is essential for D: - serine-dependent GluD2 signaling in vivo, which underlies long-term depression of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses and motor coordination in developing mice
- These results lead to a model where protein and small-molecule ligands synergistically control synaptic iGluR function
Output (sent_index, trigger,
protein,
sugar,
site):
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):