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Evolutionarily conserved principles of ESCRT-III-mediated membrane remodelling revealed by a two-subunit Asgard archaeal system
Open accessPreprint — published as 10.1126/sciadv.ads5255 · Paper page
Abstract
Summary: ESCRT-III proteins assemble into composite polymers that undergo stepwise changes in composition and structure to deform membranes across the tree of life. Here, using a phylogenetic analysis we demonstrate that the two ESCRT-III proteins present in our closest archaeal relatives are evolutionarily related to B-type and A-type eukaryotic paralogues, which initiate and execute membrane remodelling, respectively. This deep homology is reflected in ESCRT-III structure and function as demonstrated by the fact that ESCRT-IIIB assembles into parallel arrays on planar membranes to initiate membrane deformation, and is required to recruit ESCRT-IIIA to generate composite polymers. ESCRT-IIIA homopolymers can then remodel membranes into tubes, as a likely prelude to scission. Taken together, this analysis reveals a set of conserved principles governing ESCRT-III-dependent membrane remodelling that first emerged with the evolution of a two-component ESCRT-III system in the Asgard archaea, and which continue to underlie complex multi-component, ESCRT-III-dependent membrane remodelling in eukaryotes.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Souza, D. P., Espadas, J., Chaaban, S., Moody, E. R. R., Hatano, T., Balasubramanian, M., Williams, T. A., Roux, A., & Baum, B.
- Affiliations
- University of Geneva (CH)
- MRC Laboratory of Molecular Biology (GB)
- University of Bristol (GB)
- University of Warwick (GB)
- Corresponding author
- Baum, Buzz
- ORCID
- Venue
- Science Advances
- Publisher
- openRxiv
- Published
- 2024-07-02
- Volume
- 11
- Issue
- 6
- Pages
- eads5255-eads5255
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC11804906
- OpenAlex
- W4407279138
- Cited by
- 30
- References
- 1
- Citations by year
- 2026: 14 · 2025: 14 · 2024: 2
- FWCI
- 13.98
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Science Advances (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Bristol Research (University of Bristol) (publishedVersion, cc-by)
- Warwick Research Archive Portal (University of Warwick) (acceptedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Explore Bristol Research (submittedVersion, cc-by)
- Funders
- Wellcome Trust (210711/Z/18/Z, 203276/Z/16/Z)
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (200793, 189996, 310030)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- ESCRT-III, membrane remodeling, Asgard archaea, ESCRT, membrane deformation, membrane fission, phylogenetic analysis
- MeSH terms
- Archaea, Cell Membrane, Phylogeny, Evolution, Molecular, Archaeal Proteins, Endosomal Sorting Complexes Required for Transport
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