Evidence map›Paper›PMID 21628423›Full record

ArticleJournal of cell science2011

The non-receptor tyrosine kinase Lyn controls neutrophil adhesion by recruiting the CrkL-C3G complex and activating Rap1 at the leading edge.

Yuan He, Ashish Kapoor, Sara Cook, Shubai Liu, Yang Xiang, Christopher V Rao, Paul J A Kenis, Fei Wang

Open access · greenAbstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  5. Article
  6. Drugging the Mighty Neutrophil in Chronic Obstructive Pulmonary Disease.American journal of respiratory cell and molecular biology · 2019
    Article
  7. Article
  8. Src family kinases (SFKs) and cell polarity in the testis.Seminars in cell & developmental biology · 2018
    Review
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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

8 authors at 1 institution in 1 country.

Yuan HeDepartment of Cell and Developmental Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Ashish Kapoor
Sara Cook
Shubai Liu
Yang Xiang
Christopher V Rao
Paul J A Kenis
Fei Wang
University of Illinois Urbana-Champaign · US

Funding

Spatiotemporal regulation of beta adrenoceptor signaling in cardiacmyocytesR01HL082846 · NHLBI · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI XIANG, YANG K · 2006 to 2014
$3.0M
Stem cell fate and embryonic developmentR01GM083812 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI WANG, FEI · 2007 to 2014
$2.4M
Multiscale analysis of neutrophil chemotaxis and signal integrationR01GM083601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI RAO, CHRISTOPHER · 2007 to 2011
$1.4M
Polarization and directed cell movements in engineered cellular environmentsR21HD059002 · NICHD · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI LECKBAND, DEBORAH E · 2009 to 2010
$406k
NHLBI NIH HHS R01 HL082846NICHD NIH HHS HD059002NICHD NIH HHS R21 HD059002NIGMS NIH HHS GM083601NIGMS NIH HHS GM083812NIGMS NIH HHS R01 GM083601NIGMS NIH HHS R01 GM083812
6 · The paper itself

Abstract

Establishing new adhesions at the extended leading edges of motile cells is essential for stable polarity and persistent motility. Despite recent identification of signaling pathways that mediate polarity and chemotaxis in neutrophils, little is known about molecular mechanisms governing cell-extracellular-matrix (ECM) adhesion in these highly polarized and rapidly migrating cells. Here, we describe a signaling pathway in neutrophils that is essential for localized integrin activation, leading edge attachment and persistent migration during chemotaxis. This pathway depends upon G(i)-protein-mediated activation and leading edge recruitment of Lyn, a non-receptor tyrosine kinase belonging to the Src kinase family. We identified the small GTPase Rap1 as a major downstream effector of Lyn to regulate neutrophil adhesion during chemotaxis. Depletion of Lyn in neutrophil-like HL-60 cells prevented chemoattractant-induced Rap1 activation at the leading edge of the cell, whereas ectopic expression of Rap1 largely rescued the defects induced by Lyn depletion. Furthermore, Lyn controls spatial activation of Rap1 by recruiting the CrkL-C3G protein complex to the leading edge. Together, these results provide novel mechanistic insights into the poorly understood signaling network that controls leading edge adhesion during chemotaxis of neutrophils, and possibly other amoeboid cells.

Indexed as

Adaptor Proteins, Signal TransducingCell AdhesionCell LineCell MovementChemotaxisExtracellular MatrixGuanine Nucleotide-Releasing Factor 2HumansNeutrophilsNuclear ProteinsProtein BindingShelterin ComplexSignal Transductionsrc-Family KinasesTelomere-Binding ProteinsAdaptor Proteins, Signal TransducingCRKL proteinGuanine Nucleotide-Releasing Factor 2lyn protein-tyrosine kinaseNuclear ProteinsShelterin Complexsrc-Family KinasesTelomere-Binding ProteinsTERF2IP protein, human

Identifiers

PMID21628423
PMCPMC3113669
OpenAlexW2053174681

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.