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Updated: May 22, 2025

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
Published on: December 10, 2015
Dynamic structure and function of nuclear pore protein complex: Potential roles of lipid and lamins regulated nuclear
Kun-Peng Wu1, Zhi-Jie Yan1, Xiao-Xi Zhuang1
1Institute of Mechanobiology & Medical Engineering, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, 800 Dongchuan Road, Minhang, 200240 Shanghai, China.
Abstract:
The nuclear pore complex (NPC), a massive and highly sophisticated protein assembly, forms a channel embedded in the nuclear envelope (NE) of eukaryotic cells. As a critical gateway, NPC mediates the bidirectional transport of macromolecules between the cytoplasm and the nucleus. Here, we overview the structure and transport function of this protein complex, and highlight the selective barrier model of NPC transport functional modules. Nuclear membrane curvature (NMC) is a critical parameter for quantifying nuclear deformation. We discuss the mechanism by which NMC regulates dynamic NPC structure, function and distribution. Furthermore we highlight the role of two key factors, i.e. lipid composition and lamins distribution, in NMC and NPC dynamics while elucidating their regulatory mechanisms. The investigations on the dynamic structure and function of NPC modulated by NMC provide a new avenue for understanding the role of NPC in different pathological conditions. This knowledge could contribute to the development of novel therapeutic strategies.
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