Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Development. 2011 May;138(10):2133-42. doi: 10.1242/dev.057372.
The nuclear pore complex (NPC) mediates the transport of macromolecules between the nucleus and cytoplasm. Recent evidence indicates that structural nucleoporins, the building blocks of the NPC, have a variety of unanticipated cellular functions. Here, we report an unexpected tissue-specific requirement for the structural nucleoporin Seh1 during Drosophila oogenesis. Seh1 is a component of the Nup107-160 complex, the major structural subcomplex of the NPC. We demonstrate that Seh1 associates with the product of the missing oocyte (mio) gene. In Drosophila, mio regulates nuclear architecture and meiotic progression in early ovarian cysts. Like mio, seh1 has a crucial germline function during oogenesis. In both mio and seh1 mutant ovaries, a fraction of oocytes fail to maintain the meiotic cycle and develop as pseudo-nurse cells. Moreover, the accumulation of Mio protein is greatly diminished in the seh1 mutant background. Surprisingly, our characterization of a seh1 null allele indicates that, although required in the female germline, seh1 is dispensable for the development of somatic tissues. Our work represents the first examination of seh1 function within the context of a multicellular organism. In summary, our studies demonstrate that Mio is a novel interacting partner of the conserved nucleoporin Seh1 and add to the growing body of evidence that structural nucleoporins can have novel tissue-specific roles.
核孔复合体(NPC)介导核与细胞质之间的大分子运输。最近的证据表明,结构核孔蛋白,即 NPC 的构建块,具有各种意想不到的细胞功能。在这里,我们报告了结构核孔蛋白 Seh1 在果蝇卵子发生过程中的一个意外的组织特异性需求。Seh1 是 Nup107-160 复合物的组成部分,Nup107-160 复合物是 NPC 的主要结构亚基。我们证明 Seh1 与缺失卵母细胞(mio)基因的产物结合。在果蝇中,mio 调节早期卵巢小囊中的核架构和减数分裂进程。与 mio 一样,seh1 在卵子发生过程中具有至关重要的生殖系功能。在 mio 和 seh1 突变体卵巢中,一部分卵子无法维持减数分裂周期并发育为假滋养细胞。此外,在 seh1 突变体背景下,Mio 蛋白的积累大大减少。令人惊讶的是,我们对 seh1 缺失等位基因的特征分析表明,尽管 seh1 在雌性生殖系中是必需的,但它在体细胞组织的发育中是可有可无的。我们的工作代表了首次在多细胞生物体的背景下对 seh1 功能进行的研究。总之,我们的研究表明,Mio 是保守核孔蛋白 Seh1 的一个新的相互作用伙伴,并为结构核孔蛋白具有新的组织特异性作用的不断增加的证据增添了内容。