Dynamin-like protein 2

UniProtKB accession:  A0A0H3PJK4

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UniProtKB description:  The heterotetrameric DLP1(2)-DLP2(2) complex tethers liposomes and may mediate their fusion. Initial binding is probably mediated by DLP1, while DLP2 couples DLP1 subunits and increases the effective reach of the complex up to 45 nm. The role of the nucleotide is unknown. This subunit alone very weakly binds to liposomes; GTP, GDP, GMPPCP and GMPPNP do not change heterotetramer binding. Tetramerization is required for GTPase activity, suggesting the GTPase domains (dynamin-type G) from DLP1 and DLP2 must dimerize to reconstitute the GTPase active site.