Evidence map›Paper›PMID 21325030›Full record

ArticleJournal of cell science2011

Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins.

Hong Qu, Yizeng Tu, Xiaohua Shi, Hannu Larjava, Moin A Saleem, Sanford J Shattil, Koichi Fukuda, Jun Qin, Matthias Kretzler, Chuanyue Wu

Abstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing 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

58 citing papers in PubMed.

  1. FERMT2 drives anoikis resistance and peritoneal metastasis by enhancing extracellular matrix deposition in gastric cancer.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2025
    Article
  2. Article
  3. Integrins in the kidney - beyond the matrix.Nature reviews. Nephrology · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
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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

10 authors.

Hong QuDepartment of Pathology, University of Pittsburgh, Pittsburgh, PA 15261, USA.
Yizeng Tu
Xiaohua Shi
Hannu Larjava
Moin A Saleem
Sanford J Shattil
Koichi Fukuda
Jun Qin
Matthias Kretzler
Chuanyue Wu

Funding

The Interaction of TPO and Integrins in Hematopoiesis CellsP01HL078784 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GINSBERG, MARK HOWARD · 2005 to 2019
$28.3M
Discoveries at the Crossroads of Integrin and Inflammatory Signaling in PlateletsR01HL056595 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SHATTIL, SANFORD J · 1996 to 2020
$7.5M
PINCH-1 Interactions and FunctionsR01GM065188 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WU, CHUANYUE · 2002 to 2014
$3.3M
The PINCH-ILK-parvin complexes in glomerular cellsR01DK054639 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WU, CHUANYUE · 1998 to 2010
$3.2M
Periodontitis caused by kindlin-1 mutationsR01DE016099 · NIDCR · UNIVERSITY OF BRITISH COLUMBIA · PI LARJAVA, HANNU SAKARI · 2005 to 2009
$1.4M
NHLBI NIH HHS HL56595NHLBI NIH HHS HL78784NHLBI NIH HHS P01 HL078784NHLBI NIH HHS R01 HL056595NIDCR NIH HHS DE016099NIDCR NIH HHS R01 DE016099NIDDK NIH HHS DK54639NIDDK NIH HHS R01 DK054639NIGMS NIH HHS GM65188NIGMS NIH HHS R01 GM065188
6 · The paper itself

Abstract

Kindlin-2 is a FERM and PH domain-containing integrin-binding protein that is emerging as an important regulator of integrin activation. How kindlin-2 functions in integrin activation, however, is not known. We report here that kindlin-2 interacts with multiple phosphoinositides, preferentially with phosphatidylinositol 3,4,5-trisphosphate. Although integrin-binding is essential for focal adhesion localization of kindlin-2, phosphoinositide-binding is not required for this process. Using biologically and clinically relevant glomerular podocytes as a model system, we show that integrin activation and dependent processes are tightly regulated by kindlin-2: depletion of kindlin-2 reduced integrin activation, matrix adhesion and fibronectin matrix deposition, whereas overexpression of kindlin-2 promoted these processes. Furthermore, we provide evidence showing that kindlin-2 is involved in phosphoinositide-3-kinase-mediated regulation of podocyte-matrix adhesion and fibronectin matrix deposition. Mechanistically, kindlin-2 promotes integrin activation and integrin-dependent processes through interacting with both integrins and phosphoinositides. TGF-β1, a mediator of progressive glomerular failure, markedly increased the level of kindlin-2 and fibronectin matrix deposition, and the latter process was reversed by depletion of kindlin-2. Our results reveal important functions of kindlin-2 in the regulation of podocyte-matrix adhesion and matrix deposition and shed new light on the mechanism whereby kindlin-2 functions in these processes.

Indexed as

Cell AdhesionCell LineExtracellular MatrixFibronectinsHumansIntegrin beta1Integrin beta3Kidney GlomerulusMembrane ProteinsNeoplasm ProteinsPhosphatidylinositolsPodocytesProtein BindingProtein Structure, TertiaryTransforming Growth Factor beta1FERMT3 protein, humanFibronectinsIntegrin beta1Integrin beta3Membrane ProteinsNeoplasm ProteinsPhosphatidylinositolsTransforming Growth Factor beta1

Identifiers

PMID21325030
PMCPMC3048888

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.