Benjamin Vollmer

TL;DR: This work combines cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate the most comprehensive architectural model of the human nuclear pore complex to date.

TL;DR: It is shown that the nucleoporin Nup153 is required for NPC assembly during interphase but not during mitotic exit, and suggests that the nuclear transport receptor transportin and the small GTPase Ran regulate the interaction of N up153 with the membrane and, in this way, direct pore complex assembly to the nuclear envelope during inter phase.

TL;DR: It is shown that the evolutionary conserved nuclear pore protein Nup53 binds independently of other proteins to membranes, a property that is crucial for NPC assembly and conserved between yeast and vertebrates.

TL;DR: The current understanding of the membrane restructuring events involved in the formation of the nuclear membrane sheets of the envelope is reviewed, the mechanisms governing nuclear pore complex assembly and integration in the nascent nuclear membranes are reviewed, and the regulated coordination of these events with chromatin de-condensation is reviewed.

TL;DR: A single viral protein can mediate all events necessary for membrane budding and abscission, and pUL34 recruits pUL31 to the membrane, which, on its own, deforms membranes to produce nuclear envelope vesicles.