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Journal Article

Actin assembly ruptures the nuclear envelope by prying the lamina away from nuclear pores and nuclear membranes in starfish oocytes.

MPS-Authors
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Avilov,  I.
Research Group of Cytoskeletal Dynamics in Oocytes, MPI for Biophysical Chemistry, Max Planck Society;

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Lenart,  P.
Research Group of Cytoskeletal Dynamics in Oocytes, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Wesolowska, N., Avilov, I., Machado, P., Geiss, C., Kondo, H., Mori, M., et al. (2020). Actin assembly ruptures the nuclear envelope by prying the lamina away from nuclear pores and nuclear membranes in starfish oocytes. eLife, 9: e49774. doi:10.7554/eLife.49774.


Cite as: https://hdl.handle.net/21.11116/0000-0005-99B0-7
Abstract
The nucleus of oocytes (germinal vesicle) is unusually large and its nuclear envelope (NE) is densely packed with nuclear pore complexes (NPCs) stockpiled for embryonic development. We showed that breakdown of this specialized NE is mediated by an Arp2/3-nucleated F-actin 'shell' in starfish oocytes, in contrast to microtubule-driven tearing in mammalian fibroblasts. Here, we address the mechanism of F-actin-driven NE rupture by correlated live-cell, super-resolution and electron microscopy. We show that actin is nucleated within the lamina sprouting filopodia-like spikes towards the nuclear membranes. These F-actin spikes protrude pore-free nuclear membranes, whereas the adjoining membrane stretches accumulate NPCs associated with the still-intact lamina. Packed NPCs sort into a distinct membrane network, while breaks appear in ER-like, pore-free regions. Thereby, we reveal a new function for actin-mediated membrane shaping in nuclear rupture that is likely to have implications in other contexts such as nuclear rupture observed in cancer cells.