Phase separation of FG-nucleoporins in nuclear pore complexes

Author(s):  
Niharika Nag ◽  
Santanu Sasidharan ◽  
Vladimir N. Uversky ◽  
Prakash Saudagar ◽  
Timir Tripathi
2019 ◽  
Vol 219 (1) ◽  
Author(s):  
Dorothee Dormann

The interior of nuclear pore complexes (NPCs) is densely filled with FG-nucleoporins that form a permeability barrier of a still-obscure nature. Celetti et al. (2019. J. Cell Biol.https://doi.org/10.1083/jcb.201907157) now reveal that FG-nucleoporins can undergo liquid–liquid phase separation and form liquid droplets that mimic permeability barrier properties of intact NPCs.


Author(s):  
Brian Burke

The nuclear envelope is a complex membrane structure that forms the boundary of the nuclear compartment in eukaryotes. It regulates the passage of macromolecules between the two compartments and may be important for organizing interphase chromosome architecture. In interphase animal cells it forms a remarkably stable structure consisting of a double membrane ouerlying a protein meshwork or lamina and penetrated by nuclear pore complexes. The latter form the channels for nucleocytoplasmic exchange of macromolecules, At the onset of mitosis, however, it rapidly disassembles, the membranes fragment to yield small vesicles and the lamina, which is composed of predominantly three polypeptides, lamins R, B and C (MW approx. 74, 68 and 65 kDa respectiuely), breaks down. Lamins B and C are dispersed as monomers throughout the mitotic cytoplasm, while lamin B remains associated with the nuclear membrane vesicles.


2000 ◽  
Vol 36 ◽  
pp. 75-88 ◽  
Author(s):  
Michael P. Rout ◽  
John D. Aitchison

2021 ◽  
Vol 545 ◽  
pp. 138-144
Author(s):  
Yueyue Jing ◽  
Yilin Lv ◽  
Jingya Ye ◽  
Longfang Yao ◽  
Liwen Chen ◽  
...  

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