Evidence map›Paper›PMID 18829455›Full record

ArticleThe Journal of biological chemistry2008

Structural basis of the migfilin-filamin interaction and competition with integrin beta tails.

Yatish Lad, Pengju Jiang, Salla Ruskamo, David S Harburger, Jari Ylänne, Iain D Campbell, David A Calderwood

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

64 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Review
  3. Rational design ofNature communications · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Integrin Regulation in Immunological and Cancerous Cells and Exosomes.International journal of molecular sciences · 2021
    Review
  10. Review
  11. Review
  12. Article
  13. Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

4 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

7 authors at 3 institutions in 3 countries.

Yatish LadDepartment of Pharmacology and Interdepartmental Program in Vascular Biology and Transplantation, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Pengju Jiang
Salla Ruskamo
David S Harburger
Jari Ylänne
Iain D Campbell
David A Calderwood
University of Jyväskylä · FIUniversity of Oxford · GBYale University · US

Funding

Integrin-Filamin Interactions in Migration and SignalingR01GM068600 · NIGMS · YALE UNIVERSITY · PI CALDERWOOD, DAVID A · 2003 to 2016
$4.4M
Biotechnology and Biological Sciences Research Council BB/F006845/1NIGMS NIH HHS GM068600NIGMS NIH HHS R01 GM068600
6 · The paper itself

Abstract

A link between sites of cell adhesion and the cytoskeleton is essential for regulation of cell shape, motility, and signaling. Migfilin is a recently identified adaptor protein that localizes at cell-cell and cell-extracellular matrix adhesion sites, where it is thought to provide a link to the cytoskeleton by interacting with the actin cross-linking protein filamin. Here we have used x-ray crystallography, NMR spectroscopy, and protein-protein interaction studies to investigate the molecular basis of migfilin binding to filamin. We report that the N-terminal portion of migfilin can bind all three human filamins (FLNa, -b, or -c) and that there are multiple migfilin-binding sites in FLNa. Human filamins are composed of an N-terminal actin-binding domain followed by 24 immunoglobulin-like (IgFLN) domains and we find that migfilin binds preferentially to IgFLNa21 and more weakly to IgFLNa19 and -22. The filamin-binding site in migfilin is localized between Pro(5) and Pro(19) and binds to the CD face of the IgFLNa21 beta-sandwich. This interaction is similar to the previously characterized beta 7 integrin-IgFLNa21 interaction and migfilin and integrin beta tails can compete with one another for binding to IgFLNa21. This suggests that competition between filamin ligands for common binding sites on IgFLN domains may provide a general means of modulating filamin interactions and signaling. In this specific case, displacement of integrin tails from filamin by migfilin may provide a mechanism for switching between different integrin-cytoskeleton linkages.

Indexed as

AnimalsCell Adhesion MoleculesContractile ProteinsCytoskeletal ProteinsCytoskeletonDose-Response Relationship, DrugFilaminsHumansIntegrin beta ChainsLigandsMagnetic Resonance SpectroscopyMiceMicrofilament ProteinsModels, MolecularMolecular ConformationNIH 3T3 CellsCell Adhesion MoleculesContractile ProteinsCytoskeletal ProteinsFBLIM1 protein, humanFilaminsintegrin beta7Integrin beta ChainsLigandsMicrofilament Proteins

Identifiers

PMID18829455
PMCPMC2596399
OpenAlexW2016952508

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.