JMB-HEADER RAS-JOURNALS EIMB Pleiades Publishing

RUS

             

ENG

YearIMPACT-FACTOR
2022  1,200
2021  1,540
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 57(2023) N 4 p. 572-583; DOI 10.1134/S0026893323040131 Full Text

A.V. Orlova1*, S.G. Georgieva1, D.V. Kopytova1

Assembly and Disassembly of the Nuclear Pore Complex: A View from the Structural Side

1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia

*chipushka@gmail.com
Received - 2022-11-14; Revised - 2022-12-08; Accepted - 2022-12-08

Nucleocytoplasmic exchange in the cell occurs through the nuclear pore complexes (NPCs). NPCs are large multiprotein complexes with octagonal symmetry about their axis and imperfect mirror symmetry about a plane parallel with the nuclear envelop (NE). NPC fuses the inner and outer nuclear membranes and opens up a channel between nucleus and cytoplasm. NPC is built of nucleoporins. Each nucleoporin occurs in at least eight copies per NPC. Inside the NPC a permeability barrier forms by which NPCs can provide fast and selectable transport of molecules from one side of the nuclear membrane to the other. NPC architecture is based on hierarchical principle of organization. Nucleoporins are integrated into complexes that oligomerizes into bigger octomeric high-order structures. These structures are the main components of NPCs. In the first part of this work, the main attention is paid to NPC structure and nucleoporin properties. The second part is dedicated to mechanisms of NPC assembly and disassembly at different stages of the cell cycle.

NPC, nucleoporins, FG-repeats, Y-complex, SLiM-domain, nuclear pore complex assembly, annulate lamellae pore complexes (ALPC)



JMB-FOOTER RAS-JOURNALS