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Neurotransmission involves the exo‐endocytic cycling of synaptic vesicle ( SV ) membranes. Endocytic membrane retrieval and clathrin‐mediated  SV  reformation require curvature‐sensing and membrane‐bending  BAR  domain proteins such as endophilin A. While their ability to sense and stabilize curved membranes facilitates membrane recruitment of  BAR  domain proteins, the precise mechanisms by which they are targeted to specific sites of  SV  recycling has remained unclear. Here, we demonstrate that the multi‐domain scaffold intersectin 1 directly associates with endophilin A to facilitate vesicle uncoating at synapses. Knockout mice deficient in intersectin 1 accumulate clathrin‐coated vesicles at synapses, a phenotype akin to loss of endophilin function. Intersectin 1/endophilin A1 complex formation is mediated by direct binding of the  SH 3B domain of intersectin to a non‐canonical site on the  SH 3 domain of endophilin A1. Consistent with this, intersectin‐binding defective mutant endophilin A1 fails to rescue clathrin accumulation at neuronal synapses derived from endophilin A1‐3 triple knockout ( TKO ) mice. Our data support a model in which intersectin aids endophilin A recruitment to sites of clathrin‐mediated  SV  recycling, thereby facilitating vesicle uncoating.

Vesicle uncoating regulated by SH 3‐ SH 3 domain‐mediated complex formation between endophilin and intersectin at synapses