Evidence map›Paper›PMID 25609703›Full record

ArticleJournal of cell science2015

The focal adhesion protein PINCH-1 associates with EPLIN at integrin adhesion sites.

Esra Karaköse, Tamar Geiger, Kevin Flynn, Katrin Lorenz-Baath, Roy Zent, Matthias Mann, Reinhard Fässler

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

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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

7 authors at 2 institutions in 2 countries.

Esra KaraköseDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Tamar GeigerDepartment of Proteomics and Signal Transductions, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Kevin FlynnDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Katrin Lorenz-BaathDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Roy ZentDivision of Nephrology, Department of Medicine, Vanderbilt Medical Center, Nashville, TN, 37232, USA Department of Medicine, Nashville Veterans Affairs Medical Center, Nashville, TN, 37232, USA.
Matthias MannDepartment of Proteomics and Signal Transductions, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Reinhard FässlerDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany faessler@biochem.mpg.de.
Max Planck Institute of Biochemistry · DEVanderbilt University Medical Center · US

Funding

The Laminin Receptors in Kidney FibrosisR01DK069921 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI ROY ZENT · 2005 to 2026
$9.5M
Betal Integrin and Renal TubulogenesisR01DK075594 · NIDDK · VANDERBILT UNIVERSITY · PI ZENT, ROY · 2008 to 2015
$2.6M
Structure Function Analysis of Integrins alpha1beta1 and alpha2beta2R01DK083187 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI SANDERS, CHARLES R, ZENT, ROY · 2010 to 2013
$1.3M
The ILK/PINCH/Parvin complex in renal tubulogenesisI01BX002196 · VA · VETERANS HEALTH ADMINISTRATION · PI ZENT, ROY · 2013 to 2025
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BLRD VA I01 BX002196NIDDK NIH HHS L40 DK069221NIDDK NIH HHS R01-DK069221NIDDK NIH HHS R01 DK069921NIDDK NIH HHS R01 DK075594NIDDK NIH HHS R01-DK075594NIDDK NIH HHS R01 DK083187NIDDK NIH HHS R01-DK083187
6 · The paper itself

Abstract

PINCH-1 is a LIM-only domain protein that forms a ternary complex with integrin-linked kinase (ILK) and parvin (to form the IPP complex) downstream of integrins. Here, we demonstrate that PINCH-1 (also known as Lims1) gene ablation in the epidermis of mice caused epidermal detachment from the basement membrane, epidermal hyperthickening and progressive hair loss. PINCH-1-deficient keratinocytes also displayed profound adhesion, spreading and migration defects in vitro that were substantially more severe than those of ILK-deficient keratinocytes indicating that PINCH-1 also exerts functions in an ILK-independent manner. By isolating the PINCH-1 interactome, the LIM-domain-containing and actin-binding protein epithelial protein lost in neoplasm (EPLIN, also known as LIMA1) was identified as a new PINCH-1-associated protein. EPLIN localized, in a PINCH-1-dependent manner, to integrin adhesion sites of keratinocytes in vivo and in vitro and its depletion severely attenuated keratinocyte spreading and migration on collagen and fibronectin without affecting PINCH-1 levels in focal adhesions. Given that the low PINCH-1 levels in ILK-deficient keratinocytes were sufficient to recruit EPLIN to integrin adhesions, our findings suggest that PINCH-1 regulates integrin-mediated adhesion of keratinocytes through the interactions with ILK as well as EPLIN.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell MovementCells, CulturedCytoskeletal ProteinsFocal AdhesionsIntegrinsKeratinocytesLIM Domain ProteinsMaleMembrane ProteinsMiceMice, TransgenicAdaptor Proteins, Signal TransducingCytoskeletal ProteinsD15Ertd366e protein, mouseIntegrinsLIM Domain ProteinsLims1 protein, mouseMembrane ProteinsEPLINFocal adhesionIntegrinKeratinocyteLIMA1LIMS1PINCH-1Skin

Identifiers

PMID25609703
PMCPMC4342583
OpenAlexW2121332616

What OpenQuestion holds

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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.