Dynamin is a nerve terminal phosphoprotein with intrinsic GTPase activity which plays an important role in endocytosis. This GTPase activity is stimulated in vitro by microtubules, SH3 domain-containing proteins, phospholipids, and Protein Kinase C (PKC)-mediated phosphorylation. There are at least two distinct dynamin genes in mammals, which show 79% identity, encoding proteins Dynamin I and Dynamin II. Dynamin I is expressed almost exclusively in the central nervous system while Dynamin II expression is ubiquitous. Depolarization stimulates synaptic vesicle recycling and Dynamin I is subsequently dephosphorylated. This rapid dephosphorylation is mediated by calcineurin which acts as a switch for depolarization-initiated synaptic vesicle endocytosis. The C-terminus of dynamin contains two clusters of proline-rich SH3 domain binding proline motifs which interact with known SH3 domain proteins during tyrosine kinase receptor activation. It is reported that clone 41 detects both dynamin I and dynamin II.
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