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Description
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. Anti-Phospho Ser778 Dynamin Western blot of rat hippocampal lysate stimulated with forskolin showing specific immunolabeling of the ~95k dynamin phosphorylated at Ser778 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: (-Ptase). The blot is identical to the control except that it was incubated in (-Ptase (1200 units for 30 min) before being exposed to the Anti-Ser778 dynamin. The immunolabeling is completely eliminated by treatment with (-Ptase.