Synaptic vesicles are recycled with remarkable speed and precision in nerve
terminals. A major recycling pathway involves clathrin-mediated endocytosi
s at endocytic zones located around sites of release. Different 'accessory'
proteins linked to this pathway have been shown to alter the shape and com
position of lipid membranes, to modify membrane-coat protein interactions,
and to influence actin polymerization. These include the GTPase dynamin, th
e lysophosphatidic acid acyl transferase endophilin, and the phosphoinositi
de phosphatase synaptojanin. Protein perturbation studies in living nerve t
erminals are now beginning to link the actions of these proteins with morph
ologically defined steps of endocytosis.