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Authors:  Lennart Brodin, Joel Jakobsson, Frauke Ackermann, Fredrik Andersson, Peter Lw, Department of Neuroscience, Karolinska Institutet, Stockholm, Sweden
The molecular mechanisms underlying recycling of synaptic vesicles in nerve terminals are the subject of intense investigation. In this review we consider recent progress in this field with a focus on syndapin 1, a candidate endocytic protein distinguished by its membrane-sculpting and actin remodeling properties. Syndapin 1 interacts with dynamin and the actin-regulator N-WASP, and it contains a F-BAR domain which effectively deforms membranes. In vertebrates, perturbation of syndapin 1, or of its interaction with dynamin does not influence the clathrin-dependent pathway used for synaptic vesicle recycling at moderate rates. However, synaptic vesicle recycling during high levels of synaptic activity is markedly disrupted by these treatments. This distinct role of syndapin probably reflects an involvement in bulk endocytosis, a pathway yet to be defined in molecular terms. Additionally, on the postsynaptic side, syndapin participates in clathrin-mediated uptake of a distinct set of neurotransmitter receptors during development. The synaptic role of syndapin may be limited to vertebrates as genetic deletion of the single syndapin isoform in Drosophila does not affect synaptic function. Syndapin may thus not be regarded as a core component of the clathrin-dependent synaptic vesicle recycling machinery, because it functions in a subset of pre- and postsynaptic endocytic pathways. 

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