Apr 18, 2016

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

BioRxiv : the Preprint Server for Biology
Jeremy CarltonYolanda Olmos

Abstract

The Endosomal Sorting Complex Required for Transport-III (ESCRT-III) machinery controls nuclear envelope (NE) reformation during mitotic exit by sealing holes in the reforming NE. It also acts to repair the NE upon rupture. The ESCRT-III component CHMP7 is responsible for recruitment of ESCRT-III to this organelle. Here, we show that the N-terminus of CHMP7, comprising tandem Winged Helix (WH)-domains, is a novel membrane-binding module. This activity allows CHMP7 to bind to the Endoplasmic Reticulum (ER), an organelle contiguous with the NE, and provides a platform to direct NE-localisation of ESCRT-III during mitotic exit. Point mutations that disrupt membrane-binding prevent CHMP7 localising to the ER and its subsequent enrichment at the reforming NE. These mutations prevent both 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 nuclear biogenesis.

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Mentioned in this Paper

Establishment and Maintenance of Localization
Rupture
Phase 3 Clinical Trials
Protein Binding
Tandem Mass Spectrometry
SUN2
Endosomal Sorting Complex Required for Transport Location
Nuclear Envelope
WH/HT
Cytoplasmic

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