Dynamin : a microtubule-associated GTP-binding protein

We recently identified dynamin as a third nucleotide-sensitive microtubule-associated protein in brain tissue, in addition to kinesin and cytoplasmic dynein. Molecular cloning analysis has revealed that dynamin contains the three consensus elements characteristic of GTP-binding proteins, and biochem...

Full description

Saved in:
Bibliographic Details
Published inJournal of cell science Vol. 14; no. Supplement_14; pp. 143 - 145
Main Authors OBAR, R. A, SHPETNER, H. S, VALLEE, R. B
Format Journal Article
LanguageEnglish
Published Cambridge Company of Biologists 1991
Subjects
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Binding and carrier proteins
Biological and medical sciences
Ca(2+) Mg(2+)-ATPase - chemistry
Ca(2+) Mg(2+)-ATPase - metabolism
Dynamins
Fundamental and applied biological sciences. Psychology
Guanosine Triphosphate - metabolism
Humans
Molecular Sequence Data
Proteins
Sequence Alignment
GTP
Rat
Enzyme
Rodentia
dGTPase
Homology
Primary structure
Binding site
Binding protein
Vertebrata
Mammalia
Gene
Molecular association
Microtubule
Molecular cloning
Brain (vertebrata)
Online AccessGet full text

Cover

More Information
Summary:We recently identified dynamin as a third nucleotide-sensitive microtubule-associated protein in brain tissue, in addition to kinesin and cytoplasmic dynein. Molecular cloning analysis has revealed that dynamin contains the three consensus elements characteristic of GTP-binding proteins, and biochemical results support a role for GTP in dynamin function. Dynamin is also homologous to the Mx proteins, involved in interferon-induced viral resistance, and the product of the yeast VPS1 gene, involved in vacuolar protein sorting. These results identify a novel class of GTP-utilizing proteins, with apparently diverse functions.
ISSN:0021-9533
0269-3518
1477-9137
DOI:10.1242/jcs.1991.supplement_14.29