Abstract
The endosomal sorting complex required for transport-III (ESCRT-III) system is an ancient protein family involved in membrane remodelling. Recent phylogenetic and structural analyses reveal its conservation across the tree of life, including bacteria and archaea, suggesting an evolutionary origin predating the last universal common ancestor. These findings underscore the importance of the ESCRT-III superfamily to our origins, particularly with the recognition of their contribution to eukaryogenesis through the Asgard archaea lineage. Bacterial systems, often with a single ESCRT-III–like protein, offer a simple model for understanding how ESCRT-III can function as both membrane sensor and sculptor. This review explores the structural dynamics, evolutionary trajectories, and biological significance of ESCRT-III in bacteria and archaea. We describe how ESCRT-III polymerises and assembles conserved filaments with the coating of flat or positively curved membranes prevalent, at least in vitro. Finally, we highlight common mechanistic principles and unique adaptations that enable ESCRT-III systems to support diverse cellular processes across evolutionary domains.
| Original language | English |
|---|---|
| Article number | 103111 |
| Journal | Current Opinion in Structural Biology |
| Volume | 93 |
| Early online date | 6 Jul 2025 |
| DOIs | |
| Publication status | Published - 31 Aug 2025 |
Data Availability Statement
No data was used for the research described in the article.Acknowledgements
We would like to thank those who generously contributed electron microscopy images in Figure 3 including Carsten Sachse for PspA and Vipp1, Natalie Elia for CHMP4-7, Winfried Weissenhorn for CHMP2A/CHMP3, Frank Moss and Adam Frost for CHMP1B/IST1, Qingtao Shen for Snf7, and Adai Colom for Vipp1 atomic force microscopy images. We thank Souvik Naskar for critical review of the manuscript. We apologise to those whose work we could not include due to space limitation.Funding
TAW received support from the Gordon and Betty Moore Foundation (GBMF9741) and the John Templeton Foundation (63451). The opinions expressed in this publication are those of the authors and do not necessarily reflect the views of the John Templeton Foundation. HHL received support from Wellcome Trust Senior Research Fellowship (215553/Z/19/Z) and Discovery award (317484/Z/24/Z), and BBSRC grant (BB/W008181/1).
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology