Evidence map›Paper›PMID 21998205›Full record

ArticleMolecular biology of the cell2011

Microtubules support a disk-like septin arrangement at the plasma membrane of mammalian cells.

Mikael E Sellin, Per Holmfeldt, Sonja Stenmark, Martin Gullberg

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 61 citations in OpenAlex.

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  15. Article
  16. The Mammalian Septin Interactome.Frontiers in cell and developmental biology · 2017
    Review
  17. Article
  18. Septins guide microtubule protrusions induced by actin-depolymerizing toxins like Clostridium difficile transferase (CDT).Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. 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

4 authors at 2 institutions in 2 countries.

Mikael E SellinDepartment of Molecular Biology, Umeå University, SE-901 87 Umeå, Sweden. mikael.sellin@molbiol.umu.se
Per Holmfeldt
Sonja Stenmark
Martin Gullberg
Umeå University · SESt. Jude Children's Research Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Septin family proteins oligomerize through guanosine 5'-triphosphate-binding domains into core heteromers, which in turn polymerize at the cleavage furrow of dividing fungal and animal cells. Septin assemblies during the interphase of animal cells remain poorly defined and are the topic of this report. In this study, we developed protocols for visualization of authentic higher-order assemblies using tagged septins to effectively replace the endogenous gene product within septin core heteromers in human cells. Our analysis revealed that septins assemble into microtubule-supported, disk-like structures at the plasma membrane. In the absence of cell substrate adhesion, this is the predominant higher-order arrangement in interphase cells and each of the seven to eight septin family members expressed by the two analyzed cell types appears equally represented. However, studies of myeloid and lymphoid cell model systems revealed cell type-specific alterations of higher-order septin arrangements in response to substrate adhesion. Live-cell observations suggested that all higher-order septin assemblies are mutually exclusive with plasma membrane regions undergoing remodeling. The combined data point to a mechanism by which densely arranged cortical microtubules, which are typical for nonadhered spherical cells, support plasma membrane-bound, disk-like septin assemblies.

Indexed as

Cell AdhesionCell Cycle ProteinsCell LineCell MembraneGreen Fluorescent ProteinsHumansJurkat CellsK562 CellsLeukemia, Erythroblastic, AcuteMicrotubulesPermeabilityRecombinant ProteinsSeptinsT-LymphocytesCell Cycle Proteinsgreen fluorescent protein, Aequorea victoriaGreen Fluorescent ProteinsRecombinant ProteinsSEPTIN7 protein, humanSEPTIN9 protein, humanSeptins

Identifiers

PMID21998205
PMCPMC3226477
OpenAlexW2155813173

What OpenQuestion holds

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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.