Nuclear pore complex articles from across Nature Portfolio

Nucleoporins (NUPs) compose the nuclear pores. As skin epidermal cells switch from the progenitor state to differentiation, NUPs are downregulated without changing pore numbers. Downregulation of NUP93 is further connected to NF-kB activation.

Ader et al. find a grommet-like role for ESCRTs distinct from their nuclear envelope sealing function after spindle pole body extrusion. The grommet works with spindle pole body components that establish a diffusion barrier to maintain compartmentalization.

Romanauska and Köhler manipulate the levels of endogenously produced saturated acyl chains in yeast and show that nuclear envelope and nuclear pore complex function are uniquely sensitive to lipid acyl chain unsaturation.

We report the cryo-electron microscopy structure of native pre-60S particles trapped in the channel of the yeast nuclear pore complex, suggesting a translocation model for the export of pre-60S particles through the complex.

Early zebrafish embryos increase the size and complexity of their nuclear pore complexes, enabling efficient nuclear import of maternal transcription factors, which induces zygotic genome activation.

The nuclear pore complex (NPC) regulates transport of macromolecules into and out of the nucleus. A study now shows that mechanical force applied on the nucleus affects the transport rates across the NPC diffusion barrier, modulating the nuclear localization of certain cargos.

Nuclear pore complexes (NPCs) facilitate the fast, yet highly selective, nucleocytoplasmic transport of molecules. A recent study describes a multicolour imaging approach to chart the paths for cargo molecules through the human NPC with real-time 3D visualization of nucleocytoplasmic transport events with high spatial and temporal precision.

Zimmerli and Allegretti et al. show, in fission yeast, that nuclear pores constrict under energy deprivation or osmotic stress, which is linked to a reduction in nuclear membrane tension.

Izabela Sumara highlights the work by Beck and colleagues that identified a pathway for the biogenesis of nuclear pore complexes, which involves annulate lamellae and biomolecular condensates containing nucleoporins.

NUP98 is one of the most promiscuous fusion partners involved in leukemogenic chromosomal translocations, but the myriad of partners has long obfuscated the mechanism by which these fusion proteins drive leukemia. A new mass spectrometry–based approach has produced clues that suggest an entirely new model of leukemogenesis.