Abstract
DYNAMIN was discovered in bovine brain tissue as a nucleotide-sensitive microtubule-binding protein of relative molecular mass 100,0001. It was found to cross-link microtubules into highly ordered bundles, and appeared to have a role in intermicrotubule sliding in vitro. Cloning and sequencing of rat brain dynamin complementary DNA identified an N-terminal region of about 300 amino acids which contained the three consensus elements characteristic of GTP-binding proteins2. Extensive homology was found between this domain and the mammalian MX proteins which are involved in interferon-induced viral resistance3,4, and with the product of the VPS1 locus in Saccharomyces cerevisiae, which has been implicated both in membrane protein sorting5, and in meiotic spindle pole separation6. Dynamin-containing microtubule bundles were not observed in an immunofluorescence study of cultured mammalian cells7, but a role for a GTP-requiring protein in intermicrotubule sliding during mitosis in plants has been reported8. We report here that Drosophila melanogaster contains multiple tissue-specific and developmentally-regulated forms of dynamin, which are products of the shibire locus previously implicated in endocytic protein sorting9,10.
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Chen, M., Obar, R., Schroeder, C. et al. Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis. Nature 351, 583–586 (1991). https://doi.org/10.1038/351583a0
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DOI: https://doi.org/10.1038/351583a0
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