Dynamin is a member of a group of nerve terminal proteins called dephosphins that regulate synaptic vesicle endocytosis (Cousin et al., 2001; Graham et al., 2002; Tsuboi et al., 2002). Cyclin dependent protein kinase 5 phosphorylates dynamin at Ser774 and Ser778 that are the phosphorylation sites on dynamin phosphorylated in vivo (Tan et al., 2003). Phosphorylation of these sites on dynamin is thought to play a key role in synaptic vesicle trafficking.
