Yang Zhenyu, Liu Xianglong, Li Xiaoliang, Abbate Maurizio, Rui Han, Guan Miao, Sun Zhenglong
State Key Laboratory of Primate Biomedical Research, Institute of Primate Translational Medicine, Kunming University of Science and Technology, Kunming, China.
Yunnan Key Laboratory of Primate Biomedical Research, Kunming, China.
Heliyon. 2024 Sep 7;10(18):e36583. doi: 10.1016/j.heliyon.2024.e36583. eCollection 2024 Sep 30.
The interaction between lamin A and the cytoplasmic skeleton plays a key role in maintaining nuclear mechanical properties. However, the effect of destruction of the cytoplasmic skeleton on the 3D submicroscopic structure of lamin A has not been elucidated. In this study, we developed an image quantization algorithm to quantify changes in the submicroscopic structure of the intact lamin A 3D network within the nucleus. We used blebbistatin or nocodazole to disrupt the fibrillar structure of F-actin or tubulin, respectively, and then quantified changes in the lamin A super-resolution network structure, the morphological and mechanical properties of the nucleus and the spatial distribution of chromosomes. Ultimately, we found for the first time that disruption of the cytoplasmic skeleton changes the lamin A submicroscopic network and nuclear structural characteristics. In summary, this study contributes to understanding the trans-nuclear membrane interaction characteristics of lamin A and the cytoplasmic skeleton.
核纤层蛋白A与细胞质骨架之间的相互作用在维持核机械性能方面起着关键作用。然而，细胞质骨架破坏对核纤层蛋白A三维亚微观结构的影响尚未阐明。在本研究中，我们开发了一种图像量化算法，以量化细胞核内完整核纤层蛋白A三维网络亚微观结构的变化。我们分别使用blebbistatin或诺考达唑破坏F-肌动蛋白或微管蛋白的纤维状结构，然后量化核纤层蛋白A超分辨率网络结构、细胞核的形态和机械性能以及染色体的空间分布的变化。最终，我们首次发现细胞质骨架的破坏会改变核纤层蛋白A亚微观网络和核结构特征。总之，本研究有助于理解核纤层蛋白A与细胞质骨架的跨核膜相互作用特征。
