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Published September 16, 1997 | Published
Journal Article Open

A dynamin GTPase mutation causes a rapid and reversible temperature-inducible locomotion defect in C. elegans

Abstract

Drosophila shibire and its mammalian homologue dynamin regulate an early step in endocytosis. We identified a Caenorhabditis elegans dynamin gene, dyn-1, based upon hybridization to the Drosophila gene. The dyn-1 RNA transcripts are trans-spliced to the spliced leader 1 and undergo alternative splicing to code for either an 830- or 838-amino acid protein. These dyn-1 proteins are highly similar in amino acid sequence, structure, and size to the Drosophila and mammalian dynamins: they contain an N-terminal GTPase, a pleckstrin homology domain, and a C-terminal proline-rich domain. We isolated a recessive temperature-sensitive dyn-1 mutant containing an alteration within the GTPase domain that becomes uncoordinated when shifted to high temperature and that recovers when returned to lower temperatures, similar to D. shibire mutants. When maintained at higher temperatures, dyn-1 mutants become constipated, egg-laying defective, and produce progeny that die during embryogenesis. Using a dyn-1::lacZ gene fusion, a high level of dynamin expression was observed in motor neurons, intestine, and pharyngeal muscle. Our results suggest that dyn-1 function is required during development and for normal locomotion.

Additional Information

© 1997 The National Academy of Sciences. Contributed by Elliot M. Meyerowitz, July 17, 1997. A. M.v.d.B. thanks Paul Sternberg and the members of his lab for their advice and for sharing reagents. We are grateful to Erik Jorgensen for his valuable comments on this manuscript. Some C. elegans strains were obtained from the Caenorhabditis Genetics Center stock center. S.G.C. was supported by the Helen Hay Whitney Foundation and by the American Cancer Society (California Division). This work was supported by National Institutes of Health Program Project Grant GM40499 to E.M.M., by Public Health Services Grant DC01393 to C.I.B., and by Muscular Dystrophy Association Grant WB931203 and National Institutes of Health Grant GM51866 to A.M.v.d.B. C.I.B. is an Assistant Investigator of the Howard Hughes Medical Institute.

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August 19, 2023
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