The molecular mechanism responsible for capturing, sorting and retrieving 
vesicle membrane proteins following triggered exocytosis is not understood. Here 
we image the post-fusion release and then capture of a vesicle membrane protein, 
the vesicular acetylcholine transporter, from single vesicles in living 
neuroendocrine cells. We combine these measurements with super-resolution 
interferometric photo-activation localization microscopy and electron 
microscopy, and modelling to map the nanometer-scale topography and architecture 
of the structures responsible for the transporter's capture following 
exocytosis. We show that after exocytosis, the transporter rapidly diffuses into 
the plasma membrane, but most travels only a short distance before it is locally 
captured over a dense network of membrane-resident clathrin-coated structures. 
We propose that the extreme density of these structures acts as a short-range 
diffusion trap. They quickly sequester diffusing vesicle material and limit its 
spread across the membrane. This system could provide a means for 
clathrin-mediated endocytosis to quickly recycle vesicle proteins in highly 
excitable cells.