Clathrin-mediated endocytosis involves cycles of assembly and disassem
bly of clathrin coat components and their accessory proteins. Dephosph
orylation of rat brain extract was shown to promote the assembly of dy
namin 1, synaptojanin 1, and amphiphysin into complexes that also incl
uded clathrin and AP-2, Phosphorylation of dynamin 1 and synaptojanin
1 inhibited their binding to amphiphysin, whereas phosphorylation of a
mphiphysin inhibited its binding to AP-2 and clathrin. Thus, phosphory
lation regulates the association and dissociation cycle of the clathri
n-based endocytic machinery, and calcium-dependent dephosphorylation o
f endocytic proteins could prepare nerve terminals for a burst of endo
cytosis.