Evidence map›Paper›PMID 22891260›Full record

ArticleThe Journal of cell biology2012

Epithelial junction formation requires confinement of Cdc42 activity by a novel SH3BP1 complex.

Ahmed Elbediwy, Ceniz Zihni, Stephen J Terry, Peter Clark, Karl Matter, Maria S Balda

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 73 citations in OpenAlex.

  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. Molecular subversion of Cdc42 signalling in cancer.Biochemical Society transactions · 2021
    Review
  12. Article
  13. Article
  14. The mechanobiology of tight junctions.Biophysical reviews · 2019
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  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

6 authors at 2 institutions in 1 country.

Ahmed ElbediwyDepartment of Cell Biology, Institute of Ophthalmology, University College London, EC1V 9EL London, England, UK.
Ceniz Zihni
Stephen J Terry
Peter Clark
Karl Matter
Maria S Balda
University College London · GBImperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H002294/1Medical Research Council G0900098Wellcome Trust
6 · The paper itself

Abstract

Epithelial cell-cell adhesion and morphogenesis require dynamic control of actin-driven membrane remodeling. The Rho guanosine triphosphatase (GTPase) Cdc42 regulates sequential molecular processes during cell-cell junction formation; hence, mechanisms must exist that inactivate Cdc42 in a temporally and spatially controlled manner. In this paper, we identify SH3BP1, a GTPase-activating protein for Cdc42 and Rac, as a regulator of junction assembly and epithelial morphogenesis using a functional small interfering ribonucleic acid screen. Depletion of SH3BP1 resulted in loss of spatial control of Cdc42 activity, stalled membrane remodeling, and enhanced growth of filopodia. SH3BP1 formed a complex with JACOP/paracingulin, a junctional adaptor, and CD2AP, a scaffolding protein; both were required for normal Cdc42 signaling and junction formation. The filamentous actin-capping protein CapZ also associated with the SH3BP1 complex and was required for control of actin remodeling. Epithelial junction formation and morphogenesis thus require a dual activity complex, containing SH3BP1 and CapZ, that is recruited to sites of active membrane remodeling to guide Cdc42 signaling and cytoskeletal dynamics.

Indexed as

Actin Capping ProteinsAdaptor Proteins, Signal TransducingCaco-2 Cellscdc42 GTP-Binding ProteinCell AdhesionCytoskeletal ProteinsEpithelial CellsFemaleGTPase-Activating ProteinsHumansIntercellular JunctionsMultiprotein ComplexesRNA, Small InterferingSignal TransductionActin Capping ProteinsAdaptor Proteins, Signal TransducingCD2-associated proteincdc42 GTP-Binding ProteinCytoskeletal ProteinsGTPase-Activating ProteinsMultiprotein ComplexesRNA, Small InterferingSH3BP1 protein, human

Identifiers

PMID22891260
PMCPMC3514035
OpenAlexW2126477220

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.