Electrostatic lateral interactions drive ESCRT-III heteropolymer assembly
- Cornell University, United States
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.
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All data generated are included in the manuscript and supporting files.
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Funding
Cornell University (CU3704)
- Scott D Emr
Damon Runyon Cancer Research Foundation (DRG-2273-16)
- Sudeep Banjade
National Institute of General Medical Sciences (T32GM007273)
- Shaogeng Tang
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2019, Banjade et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Electrostatic lateral interactions drive ESCRT-III heteropolymer assembly
eLife 8:e46207.
https://doi.org/10.7554/eLife.46207
