Görlich D, Kraft R, Kostka S, Vogel F, Hartmann E, Laskey R A, Mattaj I W, Izaurralde E
Zentrum für Molekulare Biologie, Universität Heidelberg, Federal Republic of Germany.
Cell. 1996 Oct 4;87(1):21-32. doi: 10.1016/s0092-8674(00)81319-7.
Importin-alpha mediates nuclear protein import by binding nuclear localization signals and importin-beta. We find approximately 30% of SRP1p, the yeast importin-alpha, in a nuclear complex with the Saccharomyces cerevisiae nuclear cap-binding protein complex (CBC). Similarly, a large fraction of Xenopus CBC is associated with importin-alpha in the nucleus. CBC promotes nuclear export of capped U snRNAs and shuttles between nucleus and cytoplasm. The CBC-importin-alpha complex binds specifically to capped RNA, suggesting that CBC might shuttle while bound to importin-alpha. Strikingly, importin-beta binding displaces the RNA from the CBC-importin-alpha complex. Thus, the commitment of CBC for nuclear reentry triggers the release of the export substrate into the cytoplasm. We provide evidence for a mechanism that ensures that importin-mediated RNA release is a specifically cytoplasmic event.
输入蛋白α通过结合核定位信号和输入蛋白β介导核蛋白输入。我们发现,酵母输入蛋白α即SRP1p约30%存在于与酿酒酵母核帽结合蛋白复合体(CBC)形成的核复合体中。同样,非洲爪蟾CBC的很大一部分在细胞核中与输入蛋白α相关联。CBC促进加帽U snRNA的核输出,并在细胞核和细胞质之间穿梭。CBC-输入蛋白α复合体特异性结合加帽RNA,这表明CBC可能在与输入蛋白α结合时进行穿梭。引人注目的是,输入蛋白β的结合会使RNA从CBC-输入蛋白α复合体中解离。因此,CBC进入细胞核的过程会促使输出底物释放到细胞质中。我们提供了一种机制的证据,该机制确保输入蛋白介导的RNA释放是一个特定的细胞质事件。