Zaccai M, Lipshitz H D
Division of Biology 156-29, California Institute of Technology, Pasadena, USA.
Dev Genet. 1996;19(3):249-57. doi: 10.1002/(SICI)1520-6408(1996)19:3<249::AID-DVG8>3.0.CO;2-9.
Adducin is a cytoskeletal protein that can function in vitro to bundle F-actin and to control the assembly of the F-actin/spectrin cytoskeletal network. We previously reported cloning of the Drosophila Adducin-like (Add) locus [Ding et al., 1993] also referred to as hu-li tai shao (hts) [Yue and Spradling, 1992], and identification of two adducin-related protein isoforms: a 95 x 10(3) Mr form (ADD-95) and an 87 x 10(3) Mr form (ADD-87) [Zaccai and Lipshitz, 1996]. ADD-87 protein is present throughout the oocyte cortex at stages 9 and 10 of oogenesis but is restricted to its anterior pole from stage 11 onward. This ADD-87 protein localization is preceded by localization of Add-hts mRNA first to the cortex and then to the anterior pole of the oocyte. Mutation of the swallow gene results in delocalization of Add-hts mRNA and ADD-87 protein from the cortex of stage 9 and 10 oocytes, and from the anterior pole of later stage oocytes. Early embryos produced by swallow or Add-hts mutant females have severe defects in the distribution of F-actin and spectrin as well as abnormalities in nuclear division, nuclear migration, and cellularization. In addition to their cytoskeletal defects, embryos produced by swallow females have an abnormal anterior pattern because bicoid mRNA is delocalized from the anterior pole. In contrast, bicoid mRNA is still found at the anterior of embryos produced by Add-hts mothers. Thus swallow functions to restrict bicoid mRNA and Add-hts mRNA to the cortex of the oocyte. Cortical restriction of Add-hts mRNA and protein is required for the normal structure and function of the early embryonic F-actin/spectrin cytoskeleton. A defective embryonic cytoskeleton can be induced in either of two ways: (1) by delocalization of functional ADD from the oocyte cortex (as in swallow mutants), or (2) by reduction of ADD function while retaining its normal cortical localization during oogenesis (as in Add-hts mutants).
内收蛋白是一种细胞骨架蛋白,在体外可使F - 肌动蛋白成束,并控制F - 肌动蛋白/血影蛋白细胞骨架网络的组装。我们之前报道过果蝇内收蛋白样(Add)基因座的克隆[丁等人,1993年],该基因座也被称为“糊里太韶”(hts)[岳和斯普拉德林,1992年],并鉴定出两种与内收蛋白相关的蛋白质异构体:一种95×10³Mr的形式(ADD - 95)和一种87×10³Mr的形式(ADD - 87)[扎卡伊和利普希茨,1996年]。ADD - 87蛋白在卵子发生的第9和第10阶段存在于整个卵母细胞皮质,但从第11阶段起局限于其前极。这种ADD - 87蛋白的定位之前是Add - hts mRNA先定位到皮质,然后定位到卵母细胞的前极。燕子基因的突变导致Add - hts mRNA和ADD - 87蛋白从第9和第10阶段卵母细胞的皮质以及后期卵母细胞的前极错位。由燕子或Add - hts突变雌性产生的早期胚胎在F - 肌动蛋白和血影蛋白的分布上有严重缺陷,以及在核分裂、核迁移和细胞化方面存在异常。除了细胞骨架缺陷外,由燕子雌性产生的胚胎还有异常的前部模式,因为双尾mRNA从卵母细胞前极错位。相比之下,在由Add - hts母体产生的胚胎的前部仍能发现双尾mRNA。因此,燕子基因的作用是将双尾mRNA和Add - hts mRNA限制在卵母细胞的皮质。Add - hts mRNA和蛋白的皮质限制对于早期胚胎F - 肌动蛋白/血影蛋白细胞骨架的正常结构和功能是必需的。有缺陷的胚胎细胞骨架可以通过两种方式之一诱导产生:(1)通过功能性ADD从卵母细胞皮质错位(如在燕子突变体中),或(2)通过在卵子发生过程中降低ADD功能同时保持其正常的皮质定位(如在Add - hts突变体中)。