Evidence map›Paper›PMID 30333137›Full record

ArticleJournal of cell science2018

LCP1 preferentially binds clasped αMβ2 integrin and attenuates leukocyte adhesion under flow.

Hui-Yuan Tseng, Anna V Samarelli, Patricia Kammerer, Sarah Scholze, Tilman Ziegler, Roland Immler, Roy Zent, Markus Sperandio, Charles R Sanders, Reinhard Fässler and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. ILK binding to β1 integrin is indirect and mediated by kindlin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  3. Clinical Implications and Molecular Features of Extracellular Matrix Networks in Soft Tissue Sarcomas.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    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

11 authors at 4 institutions in 2 countries.

Hui-Yuan TsengDepartment of Molecular Medicine, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
Anna V SamarelliDepartment of Molecular Medicine, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
Patricia KammererDepartment of Molecular Medicine, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
Sarah ScholzeDepartment of Molecular Medicine, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
Tilman ZieglerDepartment of Molecular Medicine, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
Roland ImmlerWalter Brendel Center for Experimental Medicine, Ludwig-Maximilians-University, 81377 Munich, Germany.
Roy ZentDivision of Nephrology, Department of Medicine, Vanderbilt University, Nashville, 37232 Tennessee, USA.
Markus SperandioWalter Brendel Center for Experimental Medicine, Ludwig-Maximilians-University, 81377 Munich, Germany.ORCID 0000-0002-7689-3613
Charles R SandersDepartment of Biochemistry, Center for Structural Biology, and Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, 37232 Tennessee, USA.
Reinhard FässlerDepartment of Molecular Medicine, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
Ralph T BöttcherDepartment of Molecular Medicine, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany rboettch@biochem.mpg.de.ORCID 0000-0003-3050-7163
Max Planck Institute of Biochemistry · DEGerman Centre for Cardiovascular Research · DELudwig-Maximilians-Universität München · DEVanderbilt University · US

Funding

Betal Integrin and Renal TubulogenesisR01DK075594 · NIDDK · VANDERBILT UNIVERSITY · PI ZENT, ROY · 2008 to 2015
$2.6M
The ILK/PINCH/Parvin complex in renal tubulogenesisI01BX002196 · VA · VETERANS HEALTH ADMINISTRATION · PI ZENT, ROY · 2013 to 2025
–
BLRD VA I01 BX002196European Research Council 322652NIDDK NIH HHS R01 DK075594
6 · The paper itself

Abstract

Integrins are α/β heterodimers that interconvert between inactive and active states. In the active state the α/β cytoplasmic domains recruit integrin-activating proteins and separate the transmembrane and cytoplasmic (TMcyto) domains (unclasped TMcyto). Conversely, in the inactive state the α/β TMcyto domains bind integrin-inactivating proteins, resulting in the association of the TMcyto domains (clasped TMcyto). Here, we report the isolation of integrin cytoplasmic tail interactors using either lipid bicelle-incorporated integrin TMcyto domains (α5, αM, αIIb, β1, β2 and β3 integrin TMcyto) or a clasped, lipid bicelle-incorporated αMβ2 TMcyto. Among the proteins found to preferentially bind clasped rather than the isolated αM and β2 subunits was L-plastin (LCP1, also known as plastin-2), which binds to and maintains the inactive state of αMβ2 integrin

Indexed as

AnimalsCell AdhesionCell MembraneCytoplasmHEK293 CellsHumansLeukocytesMacrophage-1 AntigenMiceMice, Inbred C57BLMicrofilament ProteinsProtein BindingProtein ConformationRAW 264.7 CellsLCP1 protein, humanLcp1 protein, mouseMacrophage-1 AntigenMicrofilament ProteinsIntegrin inactivatorIntegrin interactomeLCP1Leukocyte adhesionProteomics

Identifiers

PMID30333137
PMCPMC6262777
OpenAlexW2897456580

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.