Evidence map›Paper›PMID 34319771›Full record

ArticleMolecular biology of the cell2021

Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.

Benjamin L Woods, Kevin S Cannon, Ellysa J D Vogt, John M Crutchley, Amy S Gladfelter

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Animal septins contain functional transmembrane domains.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. The Evolutionary Origins and Ancestral Features of Septins.bioRxiv : the preprint server for biology · 2024
    Article
  9. The evolutionary origins and ancestral features of septins.Frontiers in cell and developmental biology · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Septins From Protists to People.Frontiers in cell and developmental biology · 2021
    Review
  14. The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021
    Review
  15. 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

5 authors at 1 institution in 1 country.

Benjamin L WoodsBiology Department, University of North Carolina, Chapel Hill, NC 27599.
Kevin S CannonBiology Department, University of North Carolina, Chapel Hill, NC 27599.
Ellysa J D VogtCurriculum in Genetics and Molecular Biology, University of North Carolina, Chapel Hill, NC 27599.
John M CrutchleyBiology Department, University of North Carolina, Chapel Hill, NC 27599.
Amy S GladfelterBiology Department, University of North Carolina, Chapel Hill, NC 27599.
University of North Carolina at Chapel Hill · US

Funding

Tri-Institutional Molecular Mycology and Pathogenesis Training ProgramT32AI052080 · NIAID · DUKE UNIVERSITY · PI ANDREW ALSPAUGH, JOSEPH HEITMAN · 2003 to 2026
$8.7M
Training in Mechanistic, Interdisciplinary Studies of Biological SystemsT32GM119999 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI RAMSDEN, DALE A · 2017 to 2021
$1.2M
Geometry-dependent assembly of the septin cytoskeletonR01GM130934 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GLADFELTER, AMY S · 2019 to 2022
$1.2M
NIAID NIH HHS T32 AI052080NIGMS NIH HHS R01 GM130934NIGMS NIH HHS T32 GM119999
6 · The paper itself

Abstract

The curvature of the membrane defines cell shape. Septins are GTP-binding proteins that assemble into heteromeric complexes and polymerize into filaments at areas of micron-scale membrane curvature. An amphipathic helix (AH) domain within the septin complex is necessary and sufficient for septins to preferentially assemble onto micron-scale curvature. Here we report that the nonessential fungal septin, Shs1, also has an AH domain capable of recognizing membrane curvature. In a septin mutant strain lacking a fully functional Cdc12 AH domain (

Indexed as

Cell Cycle ProteinsCell ShapeCytoskeletal ProteinsCytoskeletonMembrane ProteinsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsCDC12 protein, S cerevisiaeCell Cycle ProteinsCytoskeletal ProteinsMembrane ProteinsSaccharomyces cerevisiae ProteinsSeptinsSHS1 protein, S cerevisiae

Identifiers

PMID34319771
PMCPMC8684760
OpenAlexW3184518921

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.