Evidence map›Paper›PMID 33147991›Full record

ArticleArteriosclerosis, thrombosis, and vascular biology2021

Junctional Localization of Septin 2 Is Required for Organization of Junctional Proteins in Static Endothelial Monolayers.

Joanna Kim, John A Cooper

Abstract read
In one paragraph

Article in Arteriosclerosis, thrombosis, and vascular biology, 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
–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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Role of Septins in Endothelial Cells and Platelets.Frontiers in cell and developmental biology · 2021
    Review
  15. 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

2 authors.

Joanna KimDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO.
John A CooperDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO.

Funding

Washington University Center for Cellular ImagingP30CA091842 · NCI · WASHINGTON UNIVERSITY · PI TIMOTHY J. EBERLEIN · 2001 to 2026
$128.0M
ACTIN ASSEMBLY AND CELL MOTILITY: MECHANISMS AND REGULATIONR35GM118171 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2016 to 2020
$2.8M
Expanding Access to Planar Illumination Microscopy in a Neuroimaging CoreR24NS086741 · NINDS · WASHINGTON UNIVERSITY · PI TAGHERT, PAUL H · 2014 to 2017
$814k
NCI NIH HHS P30 CA091842NIGMS NIH HHS R35 GM118171NINDS NIH HHS R24 NS086741
6 · The paper itself

Abstract

objectiveSeptin 2 is localized at junctions in human microvascular endothelial monolayers. The junctional localization of septin 2 is necessary for organization of cell-cell adhesion proteins of endothelial cells. Approach and Results: Septin 2 was depleted at junctions by suppression of expression using shRNA, treatment with inflammatory cytokine, TNF (tumor necrosis factor)-α, and ectopic overexpression of septin 2 phosphatidylinositol 4,5-bisphosphate binding mutant defect in interaction with plasma membrane. Under those conditions, organizations and expression levels of various junctional proteins were analyzed. Confocal images of immunofluorescence staining showed substantial disorganization of adherens junctional proteins, nectin-2 and afadin, TJP (tight junction protein), ZO (zonula occludens)-1, and intercellular adhesion protein, PECAM-1 (platelet-endothelial cell adhesion molecule-1). Immunoblots for those proteins did not show significant changes in expression except for nectin-2 that highly increased in expression. Significant differential gene expression profiles and biological pathway analysis by septin 2 suppression and by TNF-α treatment using RNA-seq showed common overlapping pathways. The commonalities in expression may be consistent with the similar effects on the overall organization of cell-cell adhesion proteins.

conclusionsLocalization of septin 2 at cell junctions are required for the arrangement of junctional proteins and the integrity of the barrier formed by endothelial monolayers.

Indexed as

Adherens JunctionsCell AdhesionCell CommunicationCells, CulturedEndothelial CellsHumansMicrofilament ProteinsMutationNectinsPhosphatidylinositol 4,5-DiphosphatePlatelet Endothelial Cell Adhesion Molecule-1SeptinsTumor Necrosis Factor-alphaZonula Occludens-1 ProteinafadinMicrofilament ProteinsNECTIN2 protein, humanNectinsPECAM1 protein, humanPhosphatidylinositol 4,5-DiphosphatePlatelet Endothelial Cell Adhesion Molecule-1SEPTIN2 protein, humanSeptinsTJP1 protein, humanTumor Necrosis Factor-alphaZonula Occludens-1 Proteinadherens junctionscadherinscytokinesendothelial cellsnectins

Identifiers

PMID33147991
PMCPMC7769918

What OpenQuestion holds

Textmetadata
LicenceTDM
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.