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ESCRT-driven mechanisms that sense and seal holes in the nuclear membranes directly monitor the nuclear transport system and the exposure of the inner nuclear membrane.

The nuclear periphery houses compositionally and functionally distinct domains, one of which provides a 'safe zone' for replication and reassembly of heterochromatic genome regions.

Microtubule nucleation from the nuclear envelope in fission yeast involves repurposing of nuclear export proteins for a non-export-related function, docking cytoplasmic proteins at nuclear pore complexes.

A computational model of fission yeast mitosis can interrogate mechanisms required for successful mitosis, the origin of spindle length fluctuations, and spindle force balance during assembly.

Interaction of HIV capsids with the cellular protein cleavage-and-polyadenylation factor 6 at the inner side of nuclear pores promotes nuclear entry of the viral replication complex in primary human macrophages.

KASH5 uses an EF-hand domain to directly interact with the light intermediate chain of dynein, promotes processive dynein motility, and facilitates dynein recruitment to the nuclear envelope during prophase I of meiosis.

In replicative ageing yeast cells, an age-dependent impediment in proper assembly of nuclear pore complexes is associated with altered nuclear transport.

A theoretical model explains how protein density and nuclear to cell volume ratio are maintained during cell growth, discusses conditions under which this breaks down, and highlights the importance of metabolites, mainly amino acids such as glutamate, in this homeostasis.

Lamin B receptor may provide a long-sought model system enabling unprecedented studies of protein quality control in the nuclear envelope of mammalian cells.

Genetic, proteomic, and structural analyses provide insight into the role of Brl1 during nuclear pore complex biogenesis, suggesting a function in the fusion of outer and inner nuclear membranes.