Nuclear envelope assembly relies on CHMP-7 in the absence of BAF-LEM-mediated hole closure

Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2023.07.06.547980v1?rss=1 Authors: Barger, S. R., Penfield, L., Bahmanyar, S. Abstract: Barrier-to-autointegration factor (BAF) is a DNA binding protein that crosslinks chromatin to assemble the nuclear envelope (NE) after mitosis. BAF also binds the Lap2b-Emerin-Man1 (LEM) domain family of NE proteins to repair interphase ruptures. The NE adaptors to ESCRTs, LEMD2-CHMP7, seal NE holes surrounding mitotic spindle microtubules (MTs), but whether NE hole closure in mitosis involves BAF-LEM binding is not known. Here, we analyze NE sealing after meiosis II in C. elegans oocytes to show that BAF-LEM binding and LEM-2-CHMP-7 have distinct roles in hole closure around spindle MTs. LEM-2/EMR-1 (emerin) function redundantly with BAF-1 to seal the NE. Compromising BAF-LEM binding revealed an additional role for EMR-1 in maintenance of the NE permeability barrier and an essential role for LEM-2-CHMP-7 in preventing NE assembly failure. The WH domain of LEM-2 recruits the majority of CHMP-7 to the NE in C. elegans and a LEM-2 -independent pool of CHMP-7, which is mostly enriched in the nucleoplasm, also contributes to NE stability. Thus, NE hole closure surrounding spindle MTs requires redundant mechanisms that safeguard against failure in NE assembly to support embryogenesis. Copy rights belong to original authors. Visit the link for more info Podcast created by Paper Player, LLC