Combined light and electron microscopy reveals a new function for Arp2/3-mediated actin assembly in nuclear envelope rupture, which leads to a separation of nuclear membranes and pores from the lamina.

Nuclear pores assemble asymmetrically, by an inside-out evagination of the inner nuclear membrane that grows in diameter and depth until it fuses with the flat outer nuclear membrane.

A protein within the nuclear membrane, MAN1, controls the expression of the circadian clock gene, BMAL1, in an example of cross-talk between two major gene regulatory pathways.

CHMP7 is phosphorylated by CDK1 upon mitotic entry, preventing interaction with LEM2 and inappropriate assembly during mitotic exit.

Biochemical and genetic approaches revealed a posttranslational mechanism controlling the abundance of SUN2, a critical nuclear envelope protein.

Cytological analyses combined with in vitro liposome reconstitution reveal that yeast SUN domain protein, Mps3, shows meiosis-specific phosphorylation in the luminal region of the nuclear envelope during meiosis for chromosome motion and nuclear envelope remodelling.

Live-cell imaging shows that the contractile acto-myosin network on the nuclear envelope remnant positions chromosomes in early mitosis to ensure efficient and correct interactions between chromosomes and the mitotic spindle.

AKAP6 is a site-specific adaptor required and sufficient to anchor centrosomal proteins and golgi to the nuclear envelope and establishes a non-centrosomal microtubule organization center (ncMTOC).

Cortical microtubule pulling forces influence nuclear envelope breakdown, while nuclear envelope remodeling, particularly lamina depolymerization, impacts mitotic spindle length during mitosis.

Myogenin promotes centrosome attenuation and establishes the nuclear envelope as the dominant microtubule organization center via the scaffold protein AKAP6, which is required for the recruitment of centrosomal proteins.