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Membrane Binding by CHMP7 Coordinates ESCRT-III-Dependent Nuclear Envelope Reformation.

Yolanda Olmos1, Anna Perdrix-Rosell1, Jeremy G Carlton1

  • 1Division of Cancer Studies, King's College London, London SE1 1UL, UK.

Current Biology : CB
|September 13, 2016
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Summary

The endosomal sorting complex required for transport-III (ESCRT-III) machinery, specifically the CHMP7 component, binds to the endoplasmic reticulum and nuclear envelope. This interaction is crucial for repairing the nuclear envelope after cell division.

Keywords:
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Biology

Background:

  • The endosomal sorting complex required for transport-III (ESCRT-III) machinery is involved in various membrane remodeling processes, including nuclear envelope (NE) repair.
  • ESCRT-III localization to the NE is dependent on the CHMP7 component, but the mechanism of NE engagement remained unclear.

Purpose of the Study:

  • To investigate the mechanism by which ESCRT-III engages with nuclear membranes.
  • To identify the specific domains and functions of CHMP7 responsible for NE localization and ESCRT-III recruitment.

Main Methods:

  • Homology modeling and structure-function analysis of CHMP7.
  • Identification and characterization of CHMP7 point mutations affecting membrane binding.
  • Analysis of ESCRT-III localization and nuclear envelope reformation in cells with mutated CHMP7.

Main Results:

  • The N terminus of CHMP7 possesses a novel membrane-binding module, enabling it to bind the ER and recruit ESCRT-III to the NE.
  • Specific point mutations disrupting CHMP7's N-terminal membrane binding prevent ER localization and NE recruitment of ESCRT-III.
  • These mutations also impair the assembly of downstream ESCRT-III components and proper post-mitotic nuclear regeneration.

Conclusions:

  • CHMP7's N-terminal membrane-binding activity is essential for recruiting the ESCRT-III complex to the nuclear envelope during mitotic exit.
  • This interaction facilitates nuclear envelope repair and the establishment of nucleo-cytoplasmic compartmentalization after cell division.