Du Jing, Fan Yan-Lei, Chen Tai-Lin, Feng Xi-Qiao
Institute of Biomechanics and Medical Engineering, Department of Engineering Mechanics, Tsinghua University, Beijing, 100084, China.
Center for Nano and Micro Mechanics, Tsinghua University, Beijing, 100084, People's Republic of China.
Cytoskeleton (Hoboken). 2015 Nov;72(11):570-5. doi: 10.1002/cm.21262. Epub 2015 Dec 22.
Nuclear actin assembly in somatic cells has been an enigma for a long time. Recently, with the advancement of novel F-actin probes, researchers have started to uncover this mystery. In this study, we investigated the actin dynamics in somatic cell nuclei using two probes: Lifeact and Utr230. Surprisingly, we observed that both Lifeact and Utr230 significantly interfered with actin dynamics in cell nuclei. Moreover, these two probes induced distinct patterns of nuclear actin assembly. While Lifeact induced filamentous actin assembly in cell nuclei, Utr230 led to various patterns of actin aggregates, including fibers, small puncta, and large patches. Moreover, the interference of actin dynamics by Lifeact was limited to nuclear actin, while Utr230 induced actin aggregation in both the nucleus and cytoplasm. Using time-lapse microscopy, we found that Lifeact-induced actin fibers remained steady over hours of observation, indicating a deficiency of nuclear F-actin reorganization. These results suggest that Lifeact and Utr230 both interfere with nuclear actin dynamics but with distinct mechanisms. This is an important finding for research on nuclear actin assembly and highlights the potential value of these two probes for exploring the native mechanisms underlying nuclear actin dynamics, which appear to be altered in the presence of these probes.
长期以来,体细胞中的核肌动蛋白组装一直是个谜。最近,随着新型F-肌动蛋白探针的发展,研究人员开始揭开这个谜团。在本研究中,我们使用两种探针Lifeact和Utr230研究了体细胞细胞核中的肌动蛋白动力学。令人惊讶的是,我们观察到Lifeact和Utr230都显著干扰了细胞核中的肌动蛋白动力学。此外,这两种探针诱导了不同模式的核肌动蛋白组装。Lifeact在细胞核中诱导丝状肌动蛋白组装,而Utr230导致肌动蛋白聚集体出现各种模式,包括纤维、小斑点和大斑块。此外,Lifeact对肌动蛋白动力学的干扰仅限于核肌动蛋白,而Utr230在细胞核和细胞质中均诱导肌动蛋白聚集。通过延时显微镜观察,我们发现Lifeact诱导的肌动蛋白纤维在数小时的观察中保持稳定,这表明核F-肌动蛋白重组存在缺陷。这些结果表明,Lifeact和Utr230都干扰核肌动蛋白动力学,但机制不同。这是核肌动蛋白组装研究中的一项重要发现,突出了这两种探针在探索核肌动蛋白动力学潜在机制方面的潜在价值,而在这些探针存在的情况下,这些机制似乎发生了改变。