Biomedicine Discovery Institute, Monash University, Clayton 3168, Australia.
Cells. 2023 Jan 11;12(2):279. doi: 10.3390/cells12020279.
The cellular response to environmental stresses, such as heat and oxidative stress, is dependent on extensive trafficking of stress-signalling molecules between the cytoplasm and nucleus, which potentiates stress-activated signalling pathways, eventually resulting in cell repair or death. Although Ran-dependent nucleocytoplasmic transport mediated by members of the importin (IPO) super family of nuclear transporters is believed to be responsible for nearly all macromolecular transit between nucleus and cytoplasm, it is paradoxically known to be significantly impaired under conditions of stress. Importin 13 (IPO13) is a unique bidirectional transporter that binds to and releases cargo in a Ran-dependent manner, but in some cases, cargo release from IPO13 is affected by loading of another cargo. To investigate IPO13's role in stress-activated pathways, we performed cell-based screens to identify a multitude of binding partners of IPO13 from human brain, lung, and testes. Analysis of the IPO13 interactome intriguingly indicated more than half of the candidate binding partners to be annotated for roles in stress responses; these included the pro-apoptotic protein nuclear clusterin (nCLU), as well as the nCLU-interacting DNA repair protein KU70. Here, we show, for the first time, that unlike other IPOs which are mislocalised and non-functional, IPO13 continues to translocate between the nucleus and cytoplasm under stress, retaining the capacity to import certain cargoes, such as nCLU, but not export others, such as KU70, as shown by analysis using fluorescence recovery after photobleaching. Importantly, depletion of IPO13 reduces stress-induced import of nCLU and protects against stress-induced cell death, with concomitant protection from DNA damage during stress. Overexpression/FACS experiments demonstrate that nCLU is dependent on IPO13 to trigger stress-induced cell death via apoptosis. Taken together, these results implicate IPO13 as a novel functional nuclear transporter in cellular stress, with a key role thereby in cell fate decision.
细胞对外界环境压力(如热和氧化应激)的反应依赖于应激信号分子在细胞质和细胞核之间的广泛运输,这增强了应激激活的信号通路,最终导致细胞修复或死亡。尽管 Ran 依赖性核质转运由核转运体的进口(IPO)超级家族的成员介导,被认为是负责几乎所有核质之间的大分子转运,但在应激条件下,它被悖论地认为显著受损。进口蛋白 13(IPO13)是一种独特的双向转运体,以依赖 Ran 的方式结合和释放货物,但在某些情况下,IPO13 从货物的释放会受到另一种货物装载的影响。为了研究 IPO13 在应激激活途径中的作用,我们进行了基于细胞的筛选,以从人脑、肺和睾丸中鉴定出大量 IPO13 的结合伙伴。IPO13 相互作用组的分析令人好奇地表明,候选结合伙伴的一半以上被注释为应激反应的角色;其中包括促凋亡蛋白核聚集素(nCLU),以及与 nCLU 相互作用的 DNA 修复蛋白 KU70。在这里,我们首次表明,与其他 IPO 不同,IPO13 在应激下继续在核质之间转运,保留了导入某些货物(如 nCLU)的能力,但不能导出其他货物(如 KU70),如荧光恢复后光漂白分析所示。重要的是,IPO13 的耗竭减少了应激诱导的 nCLU 导入,并防止了应激诱导的细胞死亡,同时在应激期间保护免受 DNA 损伤。过表达/FACS 实验表明,nCLU 依赖于 IPO13 通过细胞凋亡触发应激诱导的细胞死亡。总之,这些结果表明,IPO13 是细胞应激中的一种新型功能性核转运体,在细胞命运决定中起着关键作用。