Evidence map›Paper›PMID 34869357›Full record

ReviewFrontiers in cell and developmental biology2021

The Structural Biology of Septins and Their Filaments: An Update.

Italo A Cavini, Diego A Leonardo, Higor V D Rosa, Danielle K S V Castro, Humberto D'Muniz Pereira, Napoleão F Valadares, Ana P U Araujo, Richard C Garratt

Abstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Local RhoA activation induces septin recruitment.bioRxiv : the preprint server for biology · 2025
    Article
  18. Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Article
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

8 authors.

Italo A CaviniSão Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.
Diego A LeonardoSão Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.
Higor V D RosaSão Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.
Danielle K S V CastroSão Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.
Humberto D'Muniz PereiraSão Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.
Napoleão F ValadaresDepartment of Cellular Biology, University of Brasília, Brasília, Brazil.
Ana P U AraujoSão Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.
Richard C GarrattSão Carlos Institute of Physics, University of São Paulo, São Carlos, Brazil.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order to fully understand any complex biochemical system from a mechanistic point of view, it is necessary to have access to the three-dimensional structures of the molecular components involved. Septins and their oligomers, filaments and higher-order complexes are no exception. Indeed, the spontaneous recruitment of different septin monomers to specific positions along a filament represents a fascinating example of subtle molecular recognition. Over the last few years, the amount of structural information available about these important cytoskeletal proteins has increased dramatically. This has allowed for a more detailed description of their individual domains and the different interfaces formed between them, which are the basis for stabilizing higher-order structures such as hexamers, octamers and fully formed filaments. The flexibility of these structures and the plasticity of the individual interfaces have also begun to be understood. Furthermore, recently, light has been shed on how filaments may bundle into higher-order structures by the formation of antiparallel coiled coils involving the C-terminal domains. Nevertheless, even with these advances, there is still some way to go before we fully understand how the structure and dynamics of septin assemblies are related to their physiological roles, including their interactions with biological membranes and other cytoskeletal components. In this review, we aim to bring together the various strands of structural evidence currently available into a more coherent picture. Although it would be an exaggeration to say that this is complete, recent progress seems to suggest that headway is being made in that direction.

Indexed as

coiled coilcytoskeletal proteinGTP-binding domainhetero-oligomeric complexprotein filamentseptinstructural biology

Identifiers

PMID34869357
PMCPMC8640212

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Registered trials

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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.