Evidence map›Paper›PMID 22078565›Full record

ArticleStructure (London, England : 1993)2011

Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation.

H Dhanuja Perera, Yan-Qing Ma, Jun Yang, Jamila Hirbawi, Edward F Plow, Jun Qin

Open access · greenAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.1field-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

42 citing papers in PubMed, 56 citations in OpenAlex.

  1. Kindlin Regulates Mechanosensitive Activation and Adhesion Assembly of Integrin beta6.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022
    Review
  9. ATP allosterically stabilizes integrin-linked kinase for efficient force generation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Initiation of focal adhesion assembly by talin and kindlin: A dynamic view.Protein science : a publication of the Protein Society · 2021
    Review
  15. Article
  16. Role of Kindlin-2 in cancer progression and metastasis.Annals of translational medicine · 2020
    Review
  17. Article
  18. 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

6 authors at 2 institutions in 1 country.

H Dhanuja PereraDepartment of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, 9500 Euclid Avenue, Cleveland, OH 44195, USA.
Yan-Qing Ma
Jun Yang
Jamila Hirbawi
Edward F Plow
Jun Qin
Cleveland Clinic · USCleveland Clinic Lerner College of Medicine · US

Funding

Structure Basis for Talin-mediated Integrin ActivationP01HL073311 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI BYZOVA, TATIANA V · 2004 to 2019
$27.4M
NMR Structural Elucidation of Integrin ActivationR01GM062823 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI QIN, JUN · 2002 to 2018
$5.1M
NHLBI NIH HHS P01 HL073311NIGMS NIH HHS GM62823NIGMS NIH HHS R01 GM062823
6 · The paper itself

Abstract

Kindlin-2 belongs to an emerging class of regulators for heterodimeric (α/β) integrin adhesion receptors. By binding to integrin β cytoplasmic tail via its C-terminal FERM-like domain, kindlin-2 promotes integrin activation. Intriguingly, this activation process depends on the N terminus of kindlin-2 (K2-N) that precedes the FERM domain. The molecular function of K2-N is unclear. We present the solution structure of K2-N, which displays a ubiquitin fold similar to that observed in kindlin-1. Using chemical shift mapping and mutagenesis, we found that K2-N contains a conserved positively charged surface that binds to membrane enriched with negatively charged phosphatidylinositol-(4,5)-bisphosphate. We show that while wild-type kindlin-2 is capable of promoting integrin activation, such ability is significantly reduced for its membrane-binding defective mutant. These data suggest a membrane-binding function of the ubiquitin-like domain of kindlin-2, which is likely common for all kindlins to promote their localization to the plasma membrane and control integrin activation.

Indexed as

Amino Acid SequenceCell MembraneHumansMagnetic Resonance SpectroscopyMembrane ProteinsModels, MolecularMolecular Sequence DataNeoplasm ProteinsPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein Structure, TertiaryProtein TransportSequence Homology, Amino AcidSurface PropertiesTalinFERMT3 protein, humanMembrane ProteinsNeoplasm ProteinsPlatelet Glycoprotein GPIIb-IIIa ComplexTalin

Identifiers

PMID22078565
PMCPMC3217186
OpenAlexW2008369297

What OpenQuestion holds

Textmetadata
LicenceTDM
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.