A crosstalk between β1 and β3 integrins controls glycine receptor and gephyrin trafficking at inhibitory synapses
Résumé
The regulation of glycine receptor (GlyR) number at synapses is fundamental for the efficacy of inhibition and the control of neuronal excitability in the spinal cord. GlyR accumulation at synapses depends on the scaffolding molecule gephyrin and is linked to GlyR synaptic dwell time. However, the mechanisms that tune GlyR synaptic exchanges depending on the neuronal environment are unknown. Integrins are cell adhesion molecules and signaling receptors. Using single quantum dot and FRAP imaging, we demonstrate in rats that β1 and β3 integrins regulate the synaptic dwell time of both GlyRs and gephyrin to adjust synaptic strength. β1 and β3 integrins crosstalk via calcium/calmodulin-dependent protein kinase II and adapt GlyR lateral diffusion and gephyrin-dependent trapping at synapses. This provides a mechanism to maintain or adjust the steady state of postsynaptic molecule exchanges and the level of glycinergic inhibition in response to neuron- and glia-derived signals or extracellular matrix remodeling.
Domaines
Physique [physics]
Origine : Fichiers produits par l'(les) auteur(s)
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