Evidence map›Paper›PMID 40618701›Full record

ReviewCurrent opinion in structural biology2025

The evolution and mechanism of bacterial and archaeal ESCRT-III-like systems.

Tom A Williams, Harry H Low

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  3. Article
  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Tom A WilliamsDepartment of Life Sciences, University of Bath, Bath, UK. Electronic address: thwillia@gmail.com.
Harry H LowDepartment of Infectious Disease, Imperial College, London, UK. Electronic address: h.low@imperial.ac.uk.

Funding

Wellcome Trust
6 · The paper itself

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.

Indexed as

ArchaeaBacteriaEndosomal Sorting Complexes Required for TransportEvolution, MolecularModels, MolecularEndosomal Sorting Complexes Required for Transport

Identifiers

PMID40618701
PMCPMC7619361

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.