- Vesicular PtdIns(3,4,5)P3 and Rab7 are key effectors of sea urchin zygote nuclear membrane fusion
Summary: Class-I PI3-kinases are needed for pronuclear envelope formation and fusion in sea urchin zygotes, and Rab7 GTPase and PtdIns(3,4,5)P3 directly interact during the membrane fusion process.
- SIRT2 regulates nuclear envelope reassembly through ANKLE2 deacetylation
Summary: ANKLE2 is a new SIRT2 substrate. ANKLE2 deacetylation by SIRT2 is required for normal nuclear envelope reassembly. ANKLE2 and SIRT2 depletion yield aberrant nuclear morphology also found in Parkinson's disease, progeria and aging.
- Perforating the nuclear boundary – how nuclear pore complexes assemble
Summary: Nuclear pore complexes are the gatekeepers of the nuclear envelope. We summarize how these huge structures assemble from about a thousand individual proteins and integrate into the nuclear envelope.
- ELYS regulates the localization of LBR by modulating its phosphorylation state
Highlighted Article: The nuclear envelope localization of LBR is regulated through a phosphorylation network governed by ELYS, and defects in this phosphorylation network induce the aberrant phosphorylation and mislocalization of LBR.
- Cdc48 and Ubx1 participate in a pathway associated with the inner nuclear membrane that governs Asi1 degradation
Summary: The inner nuclear membrane (INM) E3 ubiquitin ligase component Asi1 is ubiquitylated, removed from the membrane and targeted to nuclear proteasomes through a new INM-associated degradation pathway.
- The LINC and NPC relationship – it's complicated!
Summary: In this Commentary, we review for the first time, the functional associations of two integral members of the nuclear envelope, namely the linkers of the nucleoskeleton and cytoskeleton, and nuclear pore complexes.
- A mutation abolishing the ZMPSTE24 cleavage site in prelamin A causes a progeroid disorder
Highlighted article: We describe a mutation in the human lamin A/C gene that destroys the ZMPSTE24 cleavage site and causes a progeroid disorder.
- Nuclear migration events throughout development
Summary: Nuclear migration is a central part of many cell and developmental processes. A surprisingly large number of different molecular mechanisms exist to move nuclei to specific, intracellular locations.
- Impaired mechanical response of an EDMD mutation leads to motility phenotypes that are repaired by loss of prenylation
Highlighted Article: Worms expressing the L535P Emery–Dreifuss muscular dystrophy lamin mutation show muscle phenotypes and muscle-specific abnormal responses to mechanical strain, which depend on emerin and UNC-84, and are rescued by loss of prenylation.