Phosphorylated synaphin/complexin found in the brain exhibits enhanced SNARE complex binding.

The cytosolic protein synaphin/complexin critically regulates fast neurotransmitter release at the synapse by binding to SNARE complex. However, the exact mechanism of its action remains unclear, and very little is known about how it is physiologically regulated. Here we show that synaphins (Syps) 1 and 2 can be phosphorylated in vitro by protein kinase CK2 (CK2).

Direct, Ca2+-dependent interaction between tubulin and synaptotagmin I: a possible mechanism for attaching synaptic vesicles to microtubules.

The synaptic vesicle protein synaptotagmin I probably plays important roles in the synaptic vesicle cycle. However, the mechanisms of its action remain unclear. In this study, we have searched for cytoplasmic proteins that interact with synaptotagmin I.