Evidence map›Paper›PMID 22956766›Full record

ArticleMolecular biology of the cell2012

Mammalian SEPT9 isoforms direct microtubule-dependent arrangements of septin core heteromers.

Mikael E Sellin, Sonja Stenmark, Martin Gullberg

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. 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
1.9field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Septins, a cytoskeletal protein family, with emerging role in striated muscle.Journal of muscle research and cell motility · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Mammalian Septin Interactome.Frontiers in cell and developmental biology · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Cancer-Related Functions and Subcellular Localizations of Septins.Frontiers in cell and developmental biology · 2016
    Review
  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 at 2 institutions in 2 countries.

Mikael E SellinDepartment of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden.
Sonja Stenmark
Martin Gullberg
Umeå University · SEETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Septin-family proteins assemble into rod-shaped heteromeric complexes that form higher-order arrangements at the cell cortex, where they serve apparently conserved functions as diffusion barriers and molecular scaffolds. There are 13 confirmed septin paralogues in mammals, which may be ubiquitous or tissue specific. Septin hetero-oligomerization appears homology subgroup directed, which in turn determines the subunit arrangement of six- to eight-subunit core heteromers. Here we address functional properties of human SEPT9, which, due to variable mRNA splicing, exists as multiple isoforms that differ between tissues. Myeloid K562 cells express three SEPT9 isoforms, all of which have an equal propensity to hetero-oligomerize with SEPT7-containing hexamers to generate octameric heteromers. However, due to limiting amounts of SEPT9, K562 cells contain both hexameric and octameric heteromers. To generate cell lines with controllable hexamer-to-octamer ratios and that express single SEPT9 isoforms, we developed a gene product replacement strategy. By this means we identified SEPT9 isoform-specific properties that either facilitate septin heteromer polymerization along microtubules or modulate the size range of submembranous septin disks-a prevalent septin structure in nonadhered cells. Our findings show that the SEPT9 expression level directs the hexamer-to-octamer ratio, and that the isoform composition and expression level together determine higher-order arrangements of septins.

Indexed as

Protein MultimerizationAnimalsCell Cycle ProteinsCell SurvivalGene Expression Regulation, LeukemicGenes, ReporterGreen Fluorescent ProteinsHumansInterphaseK562 CellsMammalsMicrotubulesOsmolar ConcentrationPaclitaxelProtein IsoformsProtein TransportCell Cycle ProteinsGreen Fluorescent ProteinsPaclitaxelProtein IsoformsRecombinant Fusion ProteinsRNA, MessengerSEPTIN7 protein, humanSEPTIN9 protein, humanSeptins

Identifiers

PMID22956766
PMCPMC3484102
OpenAlexW2166593242

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.