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Chaperoning the nuclear envelope

Nature Cell Biology volume 24, pages 1563–1564 (2022)Cite this article

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FG-nucleoporins of the nuclear pore complexes form a permeability barrier between the nucleus and the cytosol. FG-nucleoporins contain disordered regions and are prone to aggregation. Two studies identify the chaperone DNAJB6 as a key factor that prevents aggregation of FG-nucleoporins and assists in the biogenesis of nuclear pore complexes.

A hallmark of eukaryotic cells is their compartmentalization. The nucleus is connected to the cytoplasm by nuclear pore complexes (NPCs), which regulate transport processes in both directions across the nuclear envelope. NPCs are large and complex structures that are (re-)assembled with every cell division. NPCs are composed of nucleoporins and bridge the outer and inner membrane of the nuclear envelope. The passageway is lined by FG-nucleoporins (FG-Nups) that are characterized by natively unfolded domains enriched in phenylalanine-glycine (FG) dipeptide repeats. These FG repeats form a barrier to occlude larger proteins from further entering the NPC, but they also provide docking sites for transport factors to facilitate regulated transport1. NPCs are long-lived macromolecular complexes in post-mitotic cells and, as such, accumulate damage over time. Dividing cells depend on the re-assembly or de novo biogenesis of NPCs with each cell cycle. Unsurprisingly, NPC assembly is compromised with the progression of ageing that affects nucleocytoplasmic transport2. Given that FG-Nups have highly aggregation-prone disordered regions, how they can be protected during the assembly of NPCs and which factors become limiting with ageing were unclear.

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Fig. 1: MLF2-mediated recruitment of chaperones to nuclear envelope blebs.

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  1. Department of Cell Biology, University of Bremen, Bremen, Germany

    Janine Kirstein

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  1. Janine Kirstein
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Correspondence to Janine Kirstein.

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Kirstein, J. Chaperoning the nuclear envelope. Nat Cell Biol 24, 1563–1564 (2022). https://doi.org/10.1038/s41556-022-01013-8

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