Journal
CURRENT OPINION IN CELL BIOLOGY
Volume 24, Issue 4, Pages 453-459Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.ceb.2012.06.004
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Funding
- RIKEN Special Funding for Basic Science (Cellular System and Lipid Dynamics), Extreme Photonics
- Japan Society for the Promotion of Science (JSPS)
- Council for Science and Technology Policy (CSTP)
- Grants-in-Aid for Scientific Research [24570223] Funding Source: KAKEN
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A nuclear pore complex (NPC) is a large protein assembly that mediates the nucleocytoplasmic exchange of molecules. During the cell cycle, NPCs assemble, disassemble, and dynamically change their distribution on assembled nuclear envelope (NE), whereas in post-mitosis, NPCs are extremely stable. Extensive studies on its components, structure, and building blocks allow the study of its assembly and disassembly at the molecular level. Depending on the location that the initial components of this structure are built (e.g. chromatin versus double lipid bilayers of the nuclear envelope), the regulation and the mechanism of the assembly differ. Moreover, cell cycle dynamics of NPC are linked with INM proteins, lamins, lipid membranes, and the cell cycle signal, which show that NPC dynamics are highly regulated processes.
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