Membrane binding by CHMP7 coordinates ESCRT-III dependent nuclear envelope reformation

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In addition to its role in membrane abscission during cytokinesis, viral budding, endosomal sorting and plasma membrane repair [1], the Endosomal Sorting Complex Required for Transport-III (ESCRT-III) machinery has recently been shown to seal holes in the reforming nuclear envelope (NE) during mitotic exit [2,3]. ESCRT-III also acts during interphase to repair the NE upon migration-induced rupture [4,5], highlighting its key role as an orchestrator of membrane integrity at this organelle. Whilst NE localisation of ESCRT-III is dependent upon the ESCRT-III component CHMP7 [3], it is unclear how this complex is able to engage nuclear membranes. Here, we show that the N-terminus of CHMP7 acts as a novel membrane-binding module. This membrane-binding ability allows CHMP7 to bind to the Endoplasmic Reticulum (ER), an organelle continuous with the NE, and provides a platform to direct NE-recruitment of ESCRT-III during mitotic exit. CHMP7’s N-terminus comprises tandem Winged-Helix domains [6] and by using homology modelling and structure-function analysis, we identify point mutations that disrupt membrane-binding and prevent both ER-localisation of CHMP7 and its subsequent enrichment at the reforming NE. These mutations also prevent assembly of downstream ESCRT-III components at the reforming NE and proper establishment of post-mitotic nucleo-cytoplasmic compartmentalisation. These data identify a novel membrane-binding activity within an ESCRT-III subunit that is essential for post-mitotic nuclear regeneration.
Original languageEnglish
Pages (from-to)2635-2641
Number of pages7
JournalCurrent Biology
Issue number19
Early online date8 Sept 2016
Publication statusPublished - 10 Oct 2016


  • Cell Biology
  • Nuclear Envelope


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