Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments
Open accessAbstract
The endosomal sorting complexes required for transport (ESCRTs) constitute hetero-oligomeric machines that catalyze multiple topologically similar membrane-remodeling processes. Although ESCRT-III subunits polymerize into spirals, how individual ESCRT-III subunits are activated and assembled together into a membrane-deforming filament remains unknown. Here, we determine X-ray crystal structures of the most abundant ESCRT-III subunit Snf7 in its active conformation. Using pulsed dipolar electron spin resonance spectroscopy (PDS), we show that Snf7 activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces. This promotes the assembly of Snf7 arrays with ~30 Å periodicity into a membrane-sculpting filament. Using a combination of biochemical and genetic approaches, both in vitro and in vivo, we demonstrate that mutations on these protein interfaces halt Snf7 assembly and block ESCRT function. The architecture of the activated and membrane-bound Snf7 polymer provides crucial insights into the spatially unique ESCRT-III-mediated membrane remodeling.
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The predicted interface between the Vps2 and Vps24 subunits of the ESCRT-III complex resembles the polymerization interface of a different ESCRT-III subunit Snf7, providing insight into the roles of these previously uncharacterized ESCRT-III subunits and highlighting the generality of this mode of interaction in ESCRT-III complexes.
“Our predicted interface between the Vps2 and Vps24 subunits of the ESCRT-III complex resembles the polymerization interface of a different ESCRT-III subunit Snf7 (73), providing insight into the roles of these previously uncharacterized ESCRT-III subunits, and highlighting the generality of this mode of interaction in ESCRT-III complexes.”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [73]
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References 57 · Cited by 156
Research works printed but not linked: 1
- Gamliel D Freed JH 1990 Theory of 2-dimensional ESR with nuclear moduation Journal of Magnetic Resonance 89 60 93
- Authors
- Tang, S., Henne, W. M., Borbat, P. P., Buchkovich, N. J., Freed, J. H., Mao, Y., Fromme, J. C., & Emr, S. D.
- Affiliations
- Cornell University (US)
- Corresponding author
- Emr, Scott D
- ORCID
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2015-12-15
- Volume
- 4
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC4720517
- OpenAlex
- W2198297310
- Cited by
- 156
- References
- 57
- Citations by year
- 2026: 16 · 2025: 14 · 2024: 15 · 2023: 13 · 2022: 15 · 2021: 18 · 2020: 16 · 2019: 15 · 2018: 13 · 2017: 10 · 2016: 11
- FWCI
- 6.21
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Cornell University (Harry and Samuel Mann Outstanding Graduate Student Award, Sam and Nancy Fleming Research Fellowship, Research Grant, CU3704)
- National Institutes of Health (NIGMS Predoctoral Training Grant in Cellular and Molecular Biology, T32GM007273, NIGMS Grant, P41GM103521, NIBIB Grant, R01EB003150, NIGMS Grant, R01GM094347, NIGMS Grant, R01GM098621)
- American Cancer Society (Postdoctoral Fellowship, PF-12-062-01-DMC)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- ESCRT-III, Snf7, membrane remodeling, protein filament assembly, protein activation, conformational change, protein-membrane interface, protein-protein interfaces, membrane binding, endosomal sorting complex, crystal structure
- MeSH terms
- Membranes, Models, Molecular, Protein Binding, Protein Conformation, Endosomes, Spectrum Analysis, Crystallography, X-Ray, Saccharomyces cerevisiae Proteins, Mutant Proteins, Protein Multimerization, Endosomal Sorting Complexes Required for Transport
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