LOCALIZATION AND POSSIBLE FUNCTIONS OF DROSOPHILA SEPTINS
LOCALIZATION AND POSSIBLE FUNCTIONS OF DROSOPHILA SEPTINS
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DOI：
10.1091/mbc.6.12.1843
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发表时间：
1995-12-01
影响因子：
3.3
通讯作者：
PRINGLE, JR
中科院分区：
文献类型：
--
作者：
FARES, H;PEIFER, M;PRINGLE, JR
Septins是一类最初在酿酒酵母中发现的同源蛋白质家族，在酿酒酵母中，它们与‘颈丝’相关，并参与细胞质分裂和细胞表面组织的其他方面。在此，我们报道了一种果蝇黑腹果蝇的Sep1，基于它与酵母Septin的同源性。预测的Sep1氨基酸序列与已知的S(酿酒酵母Septin)的氨基酸序列有35%-42%的同源性，与另一种黑腹葡萄球菌Septin的同源性为52%，与已知的哺乳动物Septin的同源性为53%-73%。针对Sep1的抗体已被用来表征其表达和定位。这种蛋白质集中在分裂细胞和细胞化胚胎的分裂沟的前沿，这表明它在沟的形成中发挥了作用。Sep1定位的其他方面表明，它的作用与胞质分裂没有直接关系。例如，Sep1在合体胚囊胚皮层和原肠胚细胞内呈现有序的细胞周期协调重排；在胚胎背部闭合时，Sep1也集中在上皮的前缘，在胚胎神经系统的神经元中，以及在卵巢卵泡细胞的基侧表面。Sep1的分布通常与肌动蛋白重叠，但与肌动蛋白不同。免疫定位和生化实验都表明，Sep1与果仁有密切的联系，这表明果蝇的Septins和酵母中的一样，是复合体的一部分。
The septins are a family of homologous proteins that were originally identified in Saccharomyces cerevisiae, where they are associated with the ''neck filaments'' and are involved in cytokinesis and other aspects of the organization of the cell surface. We report here the identification of Sep1, a Drosophila melanogaster septin, based on its homology to the yeast septins. The predicted Sep1 amino acid sequence is 35-42% identical to the known S, cerevisiae septins; 52% identical to Pnut, a second D. melanogaster septin; and 53-73% identical to the known mammalian septins. Sep1-specific antibodies have been used to characterize its expression and localization. The protein is concentrated at the leading edge of the cleavage furrows of dividing cells and cellularizing embryos, suggesting a role in furrow formation. Other aspects of Sep1 localization suggest roles not directly related to cytokinesis. For example, Sep1 exhibits orderly, cell-cycle-coordinated rearrangements within the cortex of syncytial blastoderm embryos and in the cells of post-gastrulation embryos; Sep1 is also concentrated at the leading edge of the epithelium during dorsal closure in the embryo, in the neurons of the embryonic nervous system, and at the base-lateral surfaces of ovarian follicle cells. The distribution of Sep1 typically overlaps, but is distinct from, that of actin. Both immunolocalization and biochemical experiments show that Sep1 is intimately associated with Pnut, suggesting that the Drosophila septins, like those in yeast, function as part of a complex.