Evidence map›Paper›PMID 25957401›Full record

ReviewThe Journal of biological chemistry2015

Septin Form and Function at the Cell Cortex.

Andrew A Bridges, Amy S Gladfelter

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 151 citations in OpenAlex.

  1. TaggingbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Cylindrical Crystallization of CaInternational journal of molecular sciences · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025
    Article
  14. Anhidrosis in septin-7 autoimmunity.Clinical autonomic research : official journal of the Clinical Autonomic Research Society · 2025
    Article
  15. Article
  16. Article
  17. Septin complexes: Ahead of the curve.Cytoskeleton (Hoboken, N.J.) · 2025
    Article
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Andrew A BridgesFrom the Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire 03755.
Amy S GladfelterFrom the Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire 03755 Amy.Gladfelter@Dartmouth.edu.
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
Molecular and Cellular Biology at DartmouthT32GM008704 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1998 to 2018
$6.8M
NCI NIH HHS P30 CA023108NIGMS NIH HHS T32 GM008704PHS HHS NIGMS T32GM008704
6 · The paper itself

Abstract

Septins are GTP-binding proteins that form filaments and higher-order structures on the cell cortex of eukaryotic cells and associate with actin and microtubule cytoskeletal networks. When assembled, septins coordinate cell division and contribute to cell polarity maintenance and membrane remodeling. These functions manifest themselves via scaffolding of cytosolic proteins and cytoskeletal networks to specific locations on membranes and by forming diffusional barriers that restrict lateral diffusion of proteins embedded in membranes. Notably, many neurodegenerative diseases and cancers have been characterized as having misregulated septins, suggesting that their functions are relevant to diverse diseases. Despite the importance of septins, little is known about what features of the plasma membrane influence septin recruitment and alternatively, how septins influence plasma membrane properties. Septins have been localized to the cell cortex at the base of cilia, the mother-bud neck of yeast, and branch points of filamentous fungi and dendritic spines, in cleavage furrows, and in retracting membrane protrusions in mammalian cells. These sites all possess some degree of curvature and are likely composed of distinct lipid pools. Depending on the context, septins may act alone or in concert with other cytoskeletal elements to influence and sense membrane properties. The degree to which septins react to and/or induce changes in shape and lipid composition are discussed here. As septins are an essential player in basic biology and disease, understanding the interplay between septins and the plasma membrane is critical and may yield new and unexpected functions.

Indexed as

AnimalsCell CycleCell DivisionCell MembraneCell PolarityCell ShapeCytoplasmHumansModels, BiologicalModels, MolecularProtein MultimerizationSeptinsSeptinscell divisioncell polaritycytokinesiscytoskeletondiffusion barriermembrane organizationscaffold proteinseptins

Identifiers

PMID25957401
PMCPMC4498057
OpenAlexW1929262591

What OpenQuestion holds

Textmetadata
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.