Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins
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
DOI:
10.1038/347256a0
Publication Date:
2003-06-12T22:51:34Z
AUTHORS (5)
ABSTRACT
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.
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