The destruction of cytoplasmic skeleton leads to the change of nuclear structure and the looseness of lamin A submicroscopic network

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.

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Publication Details

Journal
Heliyon
Published
2024-09-01
DOI
https://doi.org/10.1016/j.heliyon.2024.e36583
Citations
2
Primary Topic
Nuclear Structure and Function
Type
article
Field-Weighted Citation Impact
0.47

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article

The destruction of cytoplasmic skeleton leads to the change of nuclear structure and the looseness of lamin A submicroscopic network

Zhenglong Sun, Xianglong Liu, Maurizio Abbate, Xiaoliang Li et al.
2 citations
Heliyon
Nuclear Structure and Function
0.47
article

The destruction of cytoplasmic skeleton leads to the change of nuclear structure and the looseness of lamin A submicroscopic network

Zhenglong Sun, Xianglong Liu, Maurizio Abbate, Xiaoliang Li, Zhenyu Yang, Miao Guan, Han Rui
article en
2 citations

Abstract

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.

HeliyonVol. 10(18)
Kunming University of Science and Technology (CN), Shenzhen Bay Laboratory (CN), Carl Zeiss (China) (CN), Yunnan Yingmao Biotechnology (China) (CN)
Natural Science Foundation of Yunnan Province, Shenzhen Bay Laboratory
Openalex Percentile: Top 35%
Nuclear Structure and Function
0.47
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