Puzzling out nuclear pore complex assembly.

Autor:	Penzo A; Université Paris Cité, CNRS, Institut Jacques Monod, Paris, France., Palancade B; Université Paris Cité, CNRS, Institut Jacques Monod, Paris, France.
Jazyk:	angličtina
Zdroj:	FEBS letters [FEBS Lett] 2023 Nov; Vol. 597 (22), pp. 2705-2727. Date of Electronic Publication: 2023 Aug 15.
DOI:	10.1002/1873-3468.14713
Abstrakt:	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. (© 2023 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
Databáze:	MEDLINE
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