Electrostatic lateral interactions drive ESCRT-III heteropolymer assembly. Academic Article uri icon

Overview

abstract

  • Self-assembly of ESCRT-III complex is a critical step in all ESCRT-dependent events. ESCRT-III hetero-polymers adopt variable architectures, but the mechanisms of inter-subunit recognition in these hetero-polymers to create flexible architectures remain unclear. We demonstrate in vivo and in vitro that the Saccharomyces cerevisiae ESCRT-III subunit Snf7 uses a conserved acidic helix to recruit its partner Vps24. Charge-inversion mutations in this helix inhibit Snf7-Vps24 lateral interactions in the polymer, while rebalancing the charges rescues the functional defects. These data suggest that Snf7-Vps24 assembly occurs through electrostatic interactions on one surface, rather than through residue-to-residue specificity. We propose a model in which these cooperative electrostatic interactions in the polymer propagate to allow for specific inter-subunit recognition, while sliding of laterally interacting polymers enable changes in architecture at distinct stages of vesicle biogenesis. Our data suggest a mechanism by which interaction specificity and polymer flexibility can be coupled in membrane-remodeling heteropolymeric assemblies.

publication date

  • June 27, 2019

Research

keywords

  • Biopolymers
  • Endosomal Sorting Complexes Required for Transport
  • Static Electricity

Identity

PubMed Central ID

  • PMC6663469

Scopus Document Identifier

  • 85071887693

Digital Object Identifier (DOI)

  • 10.7554/eLife.46207

PubMed ID

  • 31246173

Additional Document Info

volume

  • 8