Evidence map›Paper›PMID 24648497›Full record

ArticleMolecular biology of the cell2014

Cell type-specific expression of SEPT3-homology subgroup members controls the subunit number of heteromeric septin complexes.

Mikael E Sellin, Sonja Stenmark, Martin Gullberg

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Curvature sensing as an emergent property of multiscale assembly of septins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. A blueprint of septin expression in human tissues.Functional & integrative genomics · 2019
    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

3 authors.

Mikael E SellinDepartment of Molecular Biology, Umeå University, SE-901 87 Umeå, SwedenInstitute of Microbiology, D-BIOL, ETH Zürich, 8093 Zürich, Switzerland.
Sonja StenmarkDepartment of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
Martin GullbergDepartment of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden martin.gullberg@molbiol.umu.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Septins are filament-forming proteins important for organizing the cortex of animal and fungal cells. In mammals, 13 septin paralogues were recently shown to assemble into core heterohexamer and heterooctamer complexes, which serve as building blocks for apolar filamentous structures that differ among cell types. To determine how tissue-specific septin paralogue expression may shape core heteromer repertoires and thereby modulate properties of septin filaments, we devised protocols to analyze native septin heteromers with distinct numbers of subunits. Our evidence based on genetically manipulated human cells supports and extends recent concepts of homology subgroup-restricted assembly into distinct categories of apolar heterohexamers and heterooctamers. We also identify a category of tetramers that have a subunit composition equivalent to an octameric building block. These atypical tetramers are prevalent in lymphocytes and neural tissues, in which octamers are abundant but hexamers are rare. Our results can be explained by tissue-specific expression of SEPT3 subgroup members: SEPT3, SEPT9, and SEPT12. These serve as cognate subunits in either heterooctamers or atypical tetramers but exhibit different preferences in various tissues. The identified tissue-specific repertoires of septin heteromers provide insights into how higher-order septin structures with differential properties and stabilities may form in diverse animal cell types.

Indexed as

Cell Line, TumorCytoskeletal ProteinsCytoskeletonHumansJurkat CellsNeuronsPolymerizationProtein AggregatesProtein IsoformsProtein Structure, TertiaryRNA InterferenceRNA, Small InterferingSeptinsT-LymphocytesCytoskeletal ProteinsProtein AggregatesProtein IsoformsRNA, Small InterferingSEPTIN12 protein, humanseptin 3SEPTIN9 protein, humanSeptins

Identifiers

PMID24648497
PMCPMC4019491

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LicenceCC BY-NC-SA
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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.