In this review, we summarize our knowledge of the mechanisms that ensure the biogenesis of nuclear pore complexes (NPCs), the largest nonpolymeric multiprotein assemblies in eukaryotes. We discuss the challenges related to the synthesis of subunits (i.e., nucleoporins), their association into oligomers and the insertion of NPCs into nuclear envelopes, drawing parallels with the assembly of other multiprotein complexes.

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.