Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis.

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