Evidence map›Paper›PMID 23823319›Full record

ArticleBlood2013

The β2 integrin-kindlin-3 interaction is essential for T-cell homing but dispensable for T-cell activation in vivo.

Vicky Louise Morrison, Matthew MacPherson, Terhi Savinko, Hwee San Lek, Alan Prescott, Susanna Carola Fagerholm

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.2field-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

44 citing papers in PubMed, 66 citations in OpenAlex.

  1. Trial
  2. Structural basis of kindlin-3 in leukocyte adhesion deficiency III.Journal of thrombosis and haemostasis : JTH · 2026
    Article
  3. Soft matter mechanics of immune cell aggregates.Journal of the Royal Society, Interface · 2025
    Article
  4. ExosomalIranian journal of public health · 2025
    Article
  5. Article
  6. Article
  7. The integrin adhesome and control of anti-tumour immunity.Biochemical Society transactions · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. β2 integrin activation and signal transduction in leukocyte recruitment.American journal of physiology. Cell physiology · 2021
    Review
  19. Article
  20. The role of βBMC immunology · 2021
    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

6 authors at 3 institutions in 2 countries.

Vicky Louise MorrisonMedical Research Institute, Ninewells Hospital and Medical School, University of Dundee, Dundee, United Kingdom.
Matthew MacPherson
Terhi Savinko
Hwee San Lek
Alan Prescott
Susanna Carola Fagerholm
University of Dundee · GBHelsinki Institute of Physics · FINinewells Hospital · GB

Funding

Arthritis Research UKBiotechnology and Biological Sciences Research Council BB/G017123/1Cancer Research UKVersus Arthritis 19643
6 · The paper itself

Abstract

Kindlin-3 is mutated in the rare genetic disorder, leukocyte adhesion deficiency type III, which is characterized by deficient integrin-mediated adhesion of leukocytes and platelets. However, the specific roles of kindlin-3-β2-integrin interactions in T-cell adhesion and homing and immune responses in vivo remain unclear. Here, we show that the TTT motif in β2 integrins controls kindlin-3 binding. Mutation of the kindlin-3 binding site in β2 integrins caused a loss of firm adhesion of T cells under both static and shear flow conditions and a reduction of T-cell homing to lymph nodes in vivo. However, atomic force microscopy studies of integrin-ligand bonds revealed that initial ligand binding could still occur, and 2-dimensional T-cell migration was reduced but not abolished by the TTT/AAA mutation in the β2 integrin. Importantly, dendritic cell-mediated T-cell activation in vivo was normal in TTT/AAA β2 integrin knock-in mice. Our results reveal a selective role of the kindlin-3-integrin association for lymphocyte functions in vivo; the integrin-kindlin-3 interaction is particularly important in adhesion strengthening under shear flow, and for T-cell homing to lymph nodes, but dispensable for T cell activation which occurs in a shear-free environment.

Indexed as

Lymphocyte ActivationAnimalsCD18 AntigensCD4-Positive T-LymphocytesCell AdhesionCell MovementCytoskeletal ProteinsGlutathione TransferaseHEK293 CellsHumansMembrane ProteinsMiceMice, Inbred C57BLMice, TransgenicNeoplasm ProteinsT-LymphocytesCD18 AntigensCytoskeletal ProteinsFERMT3 protein, humanGlutathione Transferasekindlin-3 protein, mouseMembrane ProteinsNeoplasm Proteins

Identifiers

PMID23823319
PMCPMC3750339
OpenAlexW1973705216

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.