Evidence map›Paper›PMID 21255729›Full record

ArticleMolecular cell2011

Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division.

Rachel Y Samson, Takayuki Obita, Ben Hodgson, Michael K Shaw, Parkson Lee-Gau Chong, Roger L Williams, Stephen D Bell

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.6field-weighted citation impact, top 5% of its field
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

74 citing papers in PubMed, 137 citations in OpenAlex.

  1. Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Temporal and spatial coordination of DNA segregation and cell division in an archaeon.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. A self-assembling surface layer flattens the cytokinetic furrow to aid cell division in an archaeon.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. The Archaeal Cell Cycle.Annual review of cell and developmental biology · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Rachel Y SamsonSir William Dunn School of Pathology, South Parks Road, Oxford OX1 3RE, UK.
Takayuki Obita
Ben Hodgson
Michael K Shaw
Parkson Lee-Gau Chong
Roger L Williams
Stephen D Bell
MRC Laboratory of Molecular Biology · GBTemple University · US

Funding

Medical Research Council MC_U105184308Wellcome TrustWellcome Trust 083639/Z/07/ZWellcome Trust 086045/Z/08/Z
6 · The paper itself

Abstract

Members of the crenarchaeal kingdom, such as Sulfolobus, divide by binary fission yet lack genes for the otherwise near-ubiquitous tubulin and actin superfamilies of cytoskeletal proteins. Recent work has established that Sulfolobus homologs of the eukaryotic ESCRT-III and Vps4 components of the ESCRT machinery play an important role in Sulfolobus cell division. In eukaryotes, several pathways recruit ESCRT-III proteins to their sites of action. However, the positioning determinants for archaeal ESCRT-III are not known. Here, we identify a protein, CdvA, that is responsible for recruiting Sulfolobus ESCRT-III to membranes. Overexpression of the isolated ESCRT-III domain that interacts with CdvA results in the generation of nucleoid-free cells. Furthermore, CdvA and ESCRT-III synergize to deform archaeal membranes in vitro. The structure of the CdvA/ESCRT-III interface gives insight into the evolution of the more complex and modular eukaryotic ESCRT complex.

Indexed as

Archaeal ProteinsEndosomal Sorting Complexes Required for TransportGene Expression Regulation, ArchaealLiposomesOpen Reading FramesProtein Structure, TertiarySulfolobusTranscription, GeneticArchaeal ProteinsEndosomal Sorting Complexes Required for TransportLiposomes

Identifiers

PMID21255729
PMCPMC3763469
OpenAlexW2074456081

What OpenQuestion holds

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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.