Nuclear pore complexes (NPCs) are huge protein assemblies within the nuclear envelope (NE) that serve as selective gates for macromolecular transport between nucleus and cytoplasm. When higher eukaryotic cells prepare for division, they rapidly disintegrate NPCs during NE breakdown such that nuclear and cytoplasmic components mix to enable the formation of a cytoplasmic mitotic spindle. At the end of mitosis, reassembly of NPCs is coordinated with the establishment of the NE around decondensing chromatin. We review recent progress on mitotic NPC disassembly and reassembly, focusing on vertebrate cells. We highlight novel mechanistic insights into how NPCs are rapidly disintegrated into conveniently reusable building blocks, and put divergent models of (post-)mitotic NPC assembly into a spatial and temporal context.
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http://dx.doi.org/10.1016/j.tcb.2021.06.011 | DOI Listing |
Angew Chem Int Ed Engl
January 2025
Peking University, school of materials science and engineering, CHINA.
Dynamic liquid-liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs) and associated assembly and disassembly of biomolecular condensates play crucial roles in cellular organization and metabolic networks. These processes are often regulated by supramolecular interactions. However, the complex and disordered structures of IDPs, coupled with their rapid conformational fluctuations, pose significant challenges for reconstructing supramolecularly-regulated dynamic LLPS systems and quantitatively illustrating variations in molecular interactions.
View Article and Find Full Text PDFDev Biol
December 2024
Stowers Institute for Medical Research, Kansas City, MO, 64110, USA; Howard Hughes Medical Institute, Stowers Institute for Medical Research, Kansas City, MO, 64110, USA. Electronic address:
The cell nuclei of Ophisthokonts, the eukaryotic supergroup defined by fungi and metazoans, is remarkable in the constancy of their double-membraned structure in both somatic and germ cells. Such remarkable structural conservation underscores common and ancient evolutionary origins. Yet, the dynamics of disassembly and reassembly displayed by Ophisthokont nuclei vary extensively.
View Article and Find Full Text PDFThe disassembly and reassembly of nucleosomes by histone chaperones is an essential activity during eukaryotic transcription elongation. This highly conserved process maintains chromatin integrity by transiently removing nucleosomes as barriers and then restoring them in the wake of transcription. While transcription elongation requires multiple histone chaperones, there is little understanding of how most of them function and why so many are required.
View Article and Find Full Text PDFAdv Exp Med Biol
November 2024
Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL, USA.
Eukaryotic genome is packaged into chromatin. Thus, transcription takes place in the context of chromatin that is an array of nucleosomes. Nucleosome poses a barrier for the gene regulatory factors to access DNA for transcription to occur.
View Article and Find Full Text PDFJ Mater Chem B
December 2024
Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via. Giorgieri 1, 34127 Trieste, Italy.
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