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

Nature volume 347, pages 256–261 (1990)Cite this article

Abstract

A complementary DNA encoding the D100 poly-peptide 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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Authors and Affiliations

  1. Cell Biology Group, Worcester Foundation for Experimental Biology, 222 Maple Avenue, Shrewsbury, Massachusetts, 01545, USA

    Robert A. Obar, Christine A. Collins, James A. Hammarback, Howard S. Shpetner & Richard B. Vallee

  2. Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Ward Building, 303 East Chicago Avenue, Chicago, Illinois, 60611, USA

    Christine A. Collins

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  1. Robert A. Obar
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  3. James A. Hammarback
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  4. Howard S. Shpetner
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  5. Richard B. Vallee
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Obar, R., Collins, C., Hammarback, J. et al. Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature 347, 256–261 (1990). https://doi.org/10.1038/347256a0

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