Effects of Mutant Rat Dynamin on Endocytosis

Dynamin is a 100-kD microtubule-activated GTPase. Recent evidence has revealed a high degree of sequence homology with the product of the Drosophila gene shibire, mutations in which block the recycling of synaptic vesicles and, more generally, the formation of coated and non-coated vesicles at the p...

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Bibliographic Details
Published in:The Journal of cell biology 1993-08, Vol.122 (3), p.565-578
Main Authors: Herskovits, Jonathan S., Burgess, Christopher C., Obar, Robert A., Vallee, Richard B.
Format: Article
Language:English
Subjects:
3T3 cells
Adaptor Protein Complex alpha Subunits
Adaptor Proteins, Vesicular Transport
Amino Acid Sequence
Animals
Antibodies
Antibodies - immunology
Biological and medical sciences
Ca(2+) Mg(2+)-ATPase - chemistry
Ca(2+) Mg(2+)-ATPase - genetics
Ca(2+) Mg(2+)-ATPase - immunology
Ca(2+) Mg(2+)-ATPase - physiology
Cell Line
Cell physiology
Cells
Cellular biology
Clathrin - analysis
Clathrin - immunology
COS cells
Cultured cells
Deoxyribonucleic acid
DNA
Drosophila
Drosophila Proteins
Dynamins
Endocytosis
Fundamental and applied biological sciences. Psychology
Guanosine Triphosphate - metabolism
Microscopy, Fluorescence
Microtubules
Molecular and cellular biology
Molecular Sequence Data
Mutation
Neurons
Proteins - analysis
Proteins - immunology
Rats
Rodents
Transfection
Transferrins
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Summary:Dynamin is a 100-kD microtubule-activated GTPase. Recent evidence has revealed a high degree of sequence homology with the product of the Drosophila gene shibire, mutations in which block the recycling of synaptic vesicles and, more generally, the formation of coated and non-coated vesicles at the plasma membrane. We have now transfected cultured mammalian COS-7 cells with both wild-type and mutant dynamin cDNAs. Point mutations in the GTP-binding consensus sequence elements of dynamin equivalent to dominant negative mutations in ras, and an NH2-terminal deletion of the entire GTP-binding domain of dynamin, block transferrin uptake and alter the distribution of clathrin heavy chain and α-, but not γ-, adaptin. COOH-terminal deletions reverse these effects, identifying this portion of dynamin as a site of interaction with other components of the endocytic pathway. Over-expression of neither wild-type nor mutant forms of dynamin affected the distribution of microtubules. These results demonstrate a specific role for dynamin and for GTP in the initial stages of receptor-mediated endocytosis.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.122.3.565