The destruction of cytoplasmic skeleton leads to the change of nuclear structure and the looseness of lamin A submicroscopic network
Zhenyu Yang,
Xianglong Liu,
Xiaoliang Li,
Maurizio Abbate,
Han Rui,
Miao Guan,
Zhenglong Sun
Affiliations
Zhenyu Yang
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
Xianglong Liu
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
Xiaoliang Li
ZEISS Research Microscopy Solutions, Shanghai, China
Maurizio Abbate
Arivis AG, Rostock, Germany
Han Rui
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
Miao Guan
Faculty of Life Science and Technology, Kunming University of Science and Technology, Kunming, China; Corresponding author.
Zhenglong Sun
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; Shenzhen Bay Laboratory, Shenzhen, China; Corresponding author. State Key Laboratory of Primate Biomedical Research, Institute of Primate Translational Medicine, Kunming University of Science and Technology, Kunming, China.
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.
