Bird C H, Blink E J, Hirst C E, Buzza M S, Steele P M, Sun J, Jans D A, Bird P I
Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.
Mol Cell Biol. 2001 Aug;21(16):5396-407. doi: 10.1128/MCB.21.16.5396-5407.2001.
Proteinase inhibitor 9 (PI-9) is a human serpin present in the cytoplasm of cytotoxic lymphocytes and epithelial cells. It inhibits the cytotoxic lymphocyte granule proteinase granzyme B (graB) and is thought to protect cytotoxic lymphocytes and bystander cells from graB-mediated apoptosis. Following uptake into cells, graB promotes DNA degradation, rapidly translocating to the nucleus, where it binds a nuclear component. PI-9 should therefore be found in cytotoxic lymphocyte and bystander cell nuclei to ensure complete protection against graB. Here we demonstrate by microscopy and subcellular fractionation experiments that PI-9 is present in the nuclei of human cytotoxic cells, endothelial cells, and epithelial cells. We also show that the related serpins, PI-6, monocyte neutrophil elastase inhibitor (MNEI), PI-8, plasminogen activator inhibitor 2 (PAI-2), and the viral serpin CrmA exhibit similar nucleocytoplasmic distributions. Because these serpins lack classical nuclear localization signals and are small enough to diffuse through nuclear pores, we investigated whether import occurs actively or passively. Large (approximately 70 kDa) chimeric proteins comprising PI-9, PI-6, PI-8, MNEI, or PAI-2 fused to green fluorescent protein (GFP) show similar nucleocytoplasmic distributions to the parent proteins, indicating that nuclear import is active. By contrast, CrmA-GFP is excluded from nuclei, indicating that CrmA is not actively imported. In vitro nuclear transport assays show that PI-9 accumulates at a rate above that of passive diffusion, that it requires cytosolic factors but not ATP, and that it does not bind an intranuclear component. Furthermore, PI-9 is exported from nuclei via a leptomycin B-sensitive pathway, implying involvement of the export factor Crm1p. We conclude that the nucleocytoplasmic distribution of PI-9 and related serpins involves a nonconventional nuclear import pathway and Crm1p.
蛋白酶抑制剂9(PI-9)是一种存在于细胞毒性淋巴细胞和上皮细胞胞质中的人丝氨酸蛋白酶抑制剂。它抑制细胞毒性淋巴细胞颗粒蛋白酶颗粒酶B(graB),并被认为可保护细胞毒性淋巴细胞和旁观者细胞免受graB介导的凋亡。进入细胞后,graB促进DNA降解,迅速转移至细胞核,在那里它与一种核成分结合。因此,PI-9应该存在于细胞毒性淋巴细胞和旁观者细胞核中,以确保对graB的完全保护。在这里,我们通过显微镜和亚细胞分级分离实验证明,PI-9存在于人类细胞毒性细胞、内皮细胞和上皮细胞的细胞核中。我们还表明,相关的丝氨酸蛋白酶抑制剂PI-6、单核细胞中性粒细胞弹性蛋白酶抑制剂(MNEI)、PI-8、纤溶酶原激活物抑制剂2(PAI-2)以及病毒丝氨酸蛋白酶抑制剂CrmA表现出相似的核质分布。由于这些丝氨酸蛋白酶抑制剂缺乏经典的核定位信号,且小到足以通过核孔扩散,我们研究了其导入是主动还是被动发生的。包含与绿色荧光蛋白(GFP)融合的PI-9、PI-6、PI-8、MNEI或PAI-2的大型(约70 kDa)嵌合蛋白显示出与亲本蛋白相似的核质分布,表明核输入是主动的。相比之下,CrmA-GFP被排除在细胞核之外,表明CrmA不是主动导入的。体外核转运试验表明,PI-9以高于被动扩散的速率积累,它需要胞质因子但不需要ATP,并且它不与核内成分结合。此外,PI-9通过一种对雷帕霉素B敏感的途径从细胞核输出,这意味着输出因子Crm1p参与其中。我们得出结论,PI-9和相关丝氨酸蛋白酶抑制剂的核质分布涉及一种非传统的核输入途径和Crm1p。