11 research outputs found
The nucleoporin Nup88 is interacting with nuclear lamin A
The nuclear pore protein Nup88 binds specifically lamin A, but not B-type lamins, in vitro and in vivo. Expression of green fluorescent protein–lamin A in cells causes a masking of binding sites for Nup88 antibodies, which disappears in cells expressing mutants of lamin A that are associated with laminopathic diseases
Nuclear pore complex plasticity during developmental process as revealed by super-resolution microscopy
Heterochromatic breaks move to the nuclear periphery to continue recombinational repair
Heterochromatin mostly comprises repeated sequences prone to harmful ectopic recombination during double-strand break (DSB) repair. In Drosophila cells, ‘safe’ homologous recombination (HR) repair of heterochromatic breaks relies on a specialized pathway that relocalizes damaged sequences away from the heterochromatin domain before strand invasion. Here we show that heterochromatic DSBs move to the nuclear periphery to continue HR repair. Relocalization depends on nuclear pore and inner nuclear membrane proteins (INMPs) that anchor repair sites to the nuclear periphery via the Smc5/6-interacting proteins STUbL/RENi. Both the initial block to HR progression inside the heterochromatin domain, and the targeting of repair sites to the nuclear periphery, rely on SUMO and SUMO E3 ligases. This study reveals a critical role for SUMOylation in the spatial and temporal regulation of HR repair in heterochromatin, and identifies the nuclear periphery as a specialized site for heterochromatin repair in a multicellular eukaryote