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

• DOI: 10.1038/347256a0
• Publication Date: 2003-06-12T22:51:34Z
• Authors: Robert A. Obar; Christine A. Collins; James A. Hammarback; Howard S. Shpetner; Richard B. Vallee
• Keywords: Dynamins; 0301 basic medicine; Binding Sites; Base Sequence; Chemical Phenomena; Chemistry, Physical; Molecular Sequence Data; Saccharomyces cerevisiae; Microtubules; Rats; Mice; 03 medical and health sciences; GTP-Binding Proteins; Sequence Homology, Nucleic Acid; Animals; Amino Acid Sequence; Ca(2+) Mg(2+)-ATPase; Guanosine Triphosphate; Cloning, Molecular; Dynamin I

A complementary DNA encoding the D100 polypeptide 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.