期刊
APL BIOENGINEERING
卷 6, 期 1, 页码 -出版社
AIP Publishing
DOI: 10.1063/5.0080480
关键词
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资金
- National Science Foundation [1728407]
- Directorate For Engineering
- Div Of Civil, Mechanical, & Manufact Inn [1728407] Funding Source: National Science Foundation
The nuclear pore complex is a critical protein assembly that controls nucleocytoplasmic transport by selectively allowing specific cargoes to pass through its central channel. Recent studies have also revealed that the nuclear pore complex can regulate the channel diameter based on nuclear envelope tension, thereby altering molecular transportability.
The nuclear pore complex (NPC) is a large protein assembly that perforates the nuclear envelope and provides a sole gateway for traffic between the cytoplasm and the nucleus. The NPC controls the nucleocytoplasmic transport by selectively allowing cargoes such as proteins and mRNA to pass through its central channel, thereby playing a vital role in protecting the nuclear component and regulating gene expression and protein synthesis. The selective transport through the NPC originates from its exquisite molecular structure featuring a large scaffold and the intrinsically disordered central channel domain, but the exact mechanism underlying the selective transport remains elusive and is the subject of various, often conflicting, hypotheses. Moreover, recent studies have suggested a new role for the NPC as a mechanosensor, where the NPC changes its channel diameter depending on the nuclear envelope tension, altering the molecular transportability through this nanopore. In this mini-review, we summarize the current understandings of the selective nature of the NPC and discuss its emerging role in cellular mechanotransduction. (C) 2022 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
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