Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins

A complementary DNA encoding the D100 poly-peptide of rat brain dynamin—a force-producing, microtubule-activated nucleotide triphosphatase—has been cloned and sequenced. The predicted amino acid sequence includes a guanine nucleotide-binding domain that is homologous with those of a family of antiviral factors, inducible by interferon and known as MX proteins, and with the product of the essential yeast vacuolar protein sorting gene VPS1 . These relationships imply the existence of a new family of GTPases with physiological roles that may include microtubule-based motility and protein sorting.