It is well established that protein phosphorylation has an important role in synaptic plasticity. This is achieved, in part, via the presynaptic modulation of neurotransmitter release by protein kinases and protein phosphatases. In recent years, the increase in information available about proteins that are involved in synaptic exocytosis and endocytosis has been exploited in order to study the effects of protein phosphorylation on synaptic-vesicle cycling at the molecular level. The best-characterized protein in this respect is synapsin, whose function in the release of synaptic vesicles from the reserve pool is regulated by phosphorylation. More recently, it has emerged that proteins that function at other stages of the synaptic-vesicle cycle, which include priming of vesicles for docking-fusion and endocytic recycling, are also controlled by phosphorylation. Furthermore, recent work suggests that this regulation of membrane traffic by phosphorylation also occurs postsynaptically, where it contributes to synaptic plasticity.