Puzzling out nuclear pore complex assembly

Abstract

Nuclear pore complexes (NPCs) are sophisticated multiprotein assemblies embedded within the nuclear envelope and controlling the exchanges of molecules between the cytoplasm and the nucleus. In this review, we summarize the mechanisms by which these elaborate complexes are built from their subunits, the nucleoporins, based on our ever‐growing knowledge of NPC structural organization and on the recent identification of additional features of this process. We present the constraints faced during the production of nucleoporins, their gathering into oligomeric complexes, and the formation of NPCs within nuclear envelopes, and review the cellular strategies at play, from co‐translational assembly to the enrolment of a panel of cofactors. Remarkably, the study of NPCs can inform our perception of the biogenesis of multiprotein complexes in general – and vice versa.

An Efficient Method for Isolating and Purifying Nuclei from Mice Brain for Single-Molecule Imaging Using High-Speed Atomic Force Microscopy

“…Nucleoporins are a collection of around 30 distinct proteins that are assembled inside the cell to form biological "nanomachines" that form an eightfold rotationally symmetric core 8 scaffold that can expand between 40 and 60 nm in diameter [10,[16][17][18][19]22]. Nucleoporins (Nups) can be classified into three main groups based on their localization and functions: transmembrane Nups, which are integrated into the structure of the nuclear envelope (NE); central scaffold Nups, which provide structural support; and phenylalanine-glycine (FG)-Nups, which constitute the selective barrier within NPCs [4,5,9,12,[22][23][24]. Due to the varying anchoring sites of FGs, it is likely that they create distinct FG layers along the pathway via NPCs [25].…”