Evidence map›Paper›PMID 22648415›Full record

ArticleThe Journal of biological chemistry2012

Spatial coordination of kindlin-2 with talin head domain in interaction with integrin β cytoplasmic tails.

Kamila Bledzka, Jianmin Liu, Zhen Xu, H Dhanuja Perera, Satya P Yadav, Katarzyna Bialkowska, Jun Qin, Yan-Qing Ma, Edward F Plow

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Structural basis of kindlin-3 in leukocyte adhesion deficiency III.Journal of thrombosis and haemostasis : JTH · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Kindlins as modulators of breast cancer progression.Journal of breast cancer research · 2021
    Article
  19. Article
  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

9 authors.

Kamila BledzkaDepartment of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology/NB-50, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA.
Jianmin Liu
Zhen Xu
H Dhanuja Perera
Satya P Yadav
Katarzyna Bialkowska
Jun Qin
Yan-Qing Ma
Edward F Plow

Funding

CTSA INFRASTRUCTURE FOR PEDIATRIC RESEARCHUL1RR024989 · NCRR · CASE WESTERN RESERVE UNIVERSITY · PI DAVIS, PAMELA B · 2007 to 2011
$53.7M
Structure Basis for Talin-mediated Integrin ActivationP01HL073311 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI BYZOVA, TATIANA V · 2004 to 2019
$27.4M
Activation of the beta-3 integrins: Role of the KindlinsR01HL096062 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI PLOW, EDWARD FRANKLIN · 2009 to 2022
$5.6M
NMR Structural Elucidation of Integrin ActivationR01GM062823 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI QIN, JUN · 2002 to 2018
$5.1M
NHLBI NIH HHS P01 HL073311NHLBI NIH HHS P01HL073311NHLBI NIH HHS R01 HL096062NIGMS NIH HHS R01 GM062823
6 · The paper itself

Abstract

Both talin head domain and kindlin-2 interact with integrin β cytoplasmic tails, and they function in concert to induce integrin activation. Binding of talin head domain to β cytoplasmic tails has been characterized extensively, but information on the interaction of kindin-2 with this integrin segment is limited. In this study, we systematically examine the interactions of kindlin-2 with integrin β tails. Kindlin-2 interacted well with β(1) and β(3) tails but poorly with the β(2) cytoplasmic tail. This binding selectivity was determined by the non-conserved residues, primarily the three amino acids at the extreme C terminus of the β(3) tail, and the sequence in β(2) was non-permissive. The region at the C termini of integrin β(1) and β(3) tails recognized by kindlin-2 was a binding core of 12 amino acids. Kindlin-2 and talin head do not interact with one another but can bind simultaneously to the integrin β(3) tail without enhancing or inhibiting the interaction of the other binding partner. Kindlin-2 itself failed to directly unclasp integrin α/β tail complex, indicating that kindlin-2 must cooperate with talin to support the integrin activation mechanism.

Indexed as

AnimalsBlotting, WesternCalorimetryCHO CellsChromatography, High Pressure LiquidCricetinaeCytoplasmIntegrin beta ChainsMagnetic Resonance SpectroscopyMembrane ProteinsNeoplasm ProteinsProtein Structure, TertiarySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSurface Plasmon ResonanceTalinFERMT3 protein, humanIntegrin beta ChainsMembrane ProteinsNeoplasm ProteinsTalin

Identifiers

PMID22648415
PMCPMC3397883

What OpenQuestion holds

Textmetadata
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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.