Mingot J M, Kostka S, Kraft R, Hartmann E, Görlich D
ZMBH, INF 282, D-69120 Heidelberg, Germany.
EMBO J. 2001 Jul 16;20(14):3685-94. doi: 10.1093/emboj/20.14.3685.
Importin beta-related receptors mediate translocation through nuclear pore complexes. Co-operation with the RanGTPase system allows them to bind and subsequently release their substrates on opposite sides of the nuclear envelope, which in turn ensures a directed nucleocytoplasmic transport. Here we identify a novel family member from higher eukaryotes that functions primarily, but not exclusively, in import. It accounts for nuclear accumulation of the SUMO-1/sentrin-conjugating enzyme hUBC9 and mediates import of the RBM8 (Y14) protein, and is therefore referred to as importin 13 (Imp13). Unexpectedly, Imp13 also shows export activity towards the translation initiation factor eIF1A and is thus a case where a single importin beta-like receptor transports different substrates in opposite directions. However, Imp13 operates differently from typical exportins in that the binding of eIF1A to Imp13 is only regulated indirectly by RanGTP, and the cytoplasmic release of eIF1A from Imp13 is triggered by the loading of import substrates onto Imp13.
输入蛋白β相关受体介导通过核孔复合体的转运。与RanGTP酶系统的协同作用使它们能够在核膜的两侧结合并随后释放其底物,这反过来又确保了定向的核质运输。在这里,我们鉴定了一种来自高等真核生物的新型家族成员,其主要但并非唯一地在输入过程中发挥作用。它导致SUMO-1/泛素样小分子修饰蛋白连接酶hUBC9在细胞核中积累,并介导RBM8(Y14)蛋白的输入,因此被称为输入蛋白13(Imp13)。出乎意料的是,Imp13对翻译起始因子eIF1A也表现出输出活性,因此它是一个单一的类输入蛋白β受体在相反方向转运不同底物的例子。然而,Imp13的运作方式与典型的输出蛋白不同,因为eIF1A与Imp13的结合仅由RanGTP间接调节,并且eIF1A从Imp13的细胞质释放是由输入底物加载到Imp13上触发的。