Nuclear envelope articles from across Nature Portfolio

Here the authors show that the nucleus undergoes a transient ‘metamorphosis’ within a nuclear–cytoplasmic DNA damage response linked to health and disease. Through this process, the nuclear envelope projects tubules that capture damaged DNA, mediating its repair.

Meiosis is a specialized cell division for generating germ cells. The authors show that the lipid composition in the cellular membrane influences meiosis-specific chromosomal dynamics in mouse testis.

The X-ray crystal structure of a SUN1-KASH6 complex reveals an asymmetric trimer-of-trimers LINC complex architecture that fulfils the steric requirements for its biological role in transmitting cytoskeletal forces across the nuclear envelope.

Dissection of the nuclear pore complex provides a model in which the HIV capsid enters the nucleus through karyopherin mimicry, a mechanism likely to be conserved across other viruses.

ESCRT-III seals holes in the nuclear envelope (NE). A study now shows that the Cmp7-directed ESCRT-III cascade that grommets and reseals NE holes after spindle pole body (SPB) extrusion at the end of fission yeast mitosis is complemented by the presence of a proteinaceous diffusion barrier to ensure NE integrity.

A new study shows that age-dependent nuclear remodelling in cardiomyocytes (via age-related loss of nuclear lamins) contributes to cardiac dysfunction through a process that is conserved in flies, mice and nonhuman primates.

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.

Vietri et al. show that failure to repair micronuclear membranes is caused by unrestrained activity of ESCRT-III.

Phase separation of nucleoporins supports nuclear pore complex assembly in fly embryos.

The non-specific lethal (NSL) complex is a highly conserved MOF acetyltransferase-containing complex. A recent study now shows that the NSL complex acetylates a new non-histone target, Lamin A/C and reveals the NSL complex as a crucial factor in maintaining nuclear architecture and genome integrity.