Evidence map›Paper›PMID 23437269›Full record

ArticlePloS one2013

A role of kindlin-3 in integrin αMβ2 outside-in signaling and the Syk-Vav1-Rac1/Cdc42 signaling axis.

Zhi-Hong Xue, Chen Feng, Wei-Ling Liu, Suet-Mien Tan

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Targeting Neutrophil βBiomolecules · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. β2 integrin activation and signal transduction in leukocyte recruitment.American journal of physiology. Cell physiology · 2021
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Kindlin-3 in the immune system.American journal of clinical and experimental immunology · 2014
    Review
  20. 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

4 authors at 1 institution in 1 country.

Zhi-Hong XueSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Chen Feng
Wei-Ling Liu
Suet-Mien Tan
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrins mediate cell-cell and cell-extracellular matrix attachments. Integrins are signaling receptors because their cytoplasmic tails are docking sites for cytoskeletal and signaling proteins. Kindlins are a family of band 4.1-ezrin-radixin-moesin-containing intracellular proteins. Apart from regulating integrin ligand-binding affinity, recent evidence suggests that kindlins are involved in integrin outside-in signaling. Kindlin-3 is expressed in platelets, hematopoietic cells and endothelial cells. In humans, loss of kindlin-3 expression accounts for the rare autosomal disease leukocyte adhesion deficiency (LAD) type III that is characterized by bleeding disorders and defective recruitment of leukocytes into sites of infection. Studies have shown that the loss of kindlin-3 expression leads to poor ligand-binding properties of β1, β2 and β3 integrin subfamilies. The leukocyte-restricted β2 integrin subfamily comprises four members, namely αLβ2, αMβ2, αXβ2 and αDβ2. Integrin αMβ2 mediates leukocyte adhesion, phagocytosis, degranulation and it is involved in the maintenance of immune tolerance. Here we provide further evidence that kindlin-3 is required for integrin αMβ2-mediated cell adhesion and spreading using transfected K562 cells that expressed endogenous kindlin-3 but not β2 integrins. K562 stable cell line expressing si-RNA targeting kindlin-3, but not control-si-RNA, and transfected with constitutively activated integrin αMβ2N329S adhered and spread poorly on iC3b. We also show that kindlin-3 is required for the integrin αMβ2-Syk-Vav1 signaling axis that regulates Rac1 and Cdc42 activities. These findings reinforce a role for kindlin-3 in integrin outside-in signaling.

Indexed as

Signal Transductioncdc42 GTP-Binding ProteinCell AdhesionGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsK562 CellsMacrophage-1 AntigenMembrane ProteinsNeoplasm ProteinsProtein-Tyrosine KinasesProto-Oncogene Proteins c-vavrac1 GTP-Binding Proteinrho GTP-Binding ProteinsRNA InterferenceSyk Kinasecdc42 GTP-Binding ProteinFERMT3 protein, humanIntracellular Signaling Peptides and ProteinsMacrophage-1 AntigenMembrane ProteinsNeoplasm ProteinsProtein-Tyrosine KinasesProto-Oncogene Proteins c-vavrac1 GTP-Binding Proteinrho GTP-Binding ProteinsSyk KinaseSYK protein, humanVAV1 protein, human

Identifiers

PMID23437269
PMCPMC3577682
OpenAlexW2124235481

What OpenQuestion holds

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LicenceCC BY
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.