Evidence map›Paper›PMID 25601651›Full record

ArticleThe Journal of experimental medicine2015

Moesin and myosin phosphatase confine neutrophil orientation in a chemotactic gradient.

Xiaowen Liu, Tao Yang, Koya Suzuki, Sachiko Tsukita, Masaru Ishii, Shuping Zhou, Gang Wang, Luyang Cao, Feng Qian, Shalina Taylor and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 57 citations in OpenAlex.

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  10. Frontiers in immunology · 2022
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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

17 authors at 4 institutions in 5 countries.

Xiaowen LiuDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Tao YangState Key Laboratory of Biomembrane and Membrane Biotechnology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.
Koya SuzukiLaboratory of Biological Science and Laboratory of Cellular Dynamics, Graduate School of Medicine, Osaka University, Suita 565-0871, Osaka, Japan.
Sachiko TsukitaLaboratory of Biological Science and Laboratory of Cellular Dynamics, Graduate School of Medicine, Osaka University, Suita 565-0871, Osaka, Japan.
Masaru IshiiLaboratory of Biological Science and Laboratory of Cellular Dynamics, Graduate School of Medicine, Osaka University, Suita 565-0871, Osaka, Japan.
Shuping ZhouState Key Laboratory of Biomembrane and Membrane Biotechnology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.
Gang WangDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Luyang CaoDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Feng QianDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Shalina TaylorDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Myung-Jin OhDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Irena LevitanDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Richard D YeDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Graeme K CarnegieDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Yong ZhaoState Key Laboratory of Biomembrane and Membrane Biotechnology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China jingsong@uic.edu zhaoy@ioz.ac.cn.
Asrar B MalikDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612.
Jingsong XuDepartment of Pharmacology and Department of Medicine, University of Illinois, Chicago, IL 60612 jingsong@uic.edu zhaoy@ioz.ac.cn.
University of Illinois Chicago · USChinese Academy of Sciences · CNOsaka University · JPDepartment of Physics, Mathematics and Informatics · BY

Funding

Trpm2 Regulation of Phagocyte Bactericidal Activity and Resolution of Lung InjuryP01HL077806 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MALIK, ASRAR B. · 2005 to 2019
$27.0M
Cholesterol Regulation of Endothelial K+ ChannelsR01HL073965 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI LEVITAN, IRENA · 2004 to 2024
$7.3M
Impact of dyslipidemia on endothelial biomechanicsR01HL083298 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LEVITAN, IRENA, MINSHALL, RICHARD D · 2007 to 2021
$7.0M
MOLECULAR MECHANISMS OF LEUKOCYTE ACTIVATIONR01AI033503 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI YE, RICHARD D · 1993 to 2014
$4.5M
Role of Non-muscle MLCK in Neutrophil-mediated Acute Lung InjuryR01HL095716 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI XU, JINGSONG · 2009 to 2013
$2.1M
Molecular Mechanisms of Leukocyte ActivationR56AI033503 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI YE, RICHARD D · 2009 to 2009
$393k
NHLBI NIH HHS P01 HL077806NHLBI NIH HHS R01 HL073965NHLBI NIH HHS R01 HL083298NHLBI NIH HHS R01 HL095716NIAID NIH HHS R01 AI033503NIAID NIH HHS R56 AI033503
6 · The paper itself

Abstract

Neutrophils respond to invading bacteria by adopting a polarized morphology, migrating in the correct direction, and engulfing the bacteria. How neutrophils establish and precisely orient this polarity toward pathogens remains unclear. Here we report that in resting neutrophils, the ERM (ezrin, radixin, and moesin) protein moesin in its active form (phosphorylated and membrane bound) prevented cell polarization by inhibiting the small GTPases Rac, Rho, and Cdc42. Attractant-induced activation of myosin phosphatase deactivated moesin at the prospective leading edge to break symmetry and establish polarity. Subsequent translocation of moesin to the trailing edge confined the formation of a prominent pseudopod directed toward pathogens and prevented secondary pseudopod formation in other directions. Therefore, both moesin-mediated inhibition and its localized deactivation by myosin phosphatase are essential for neutrophil polarization and effective neutrophil tracking of pathogens.

Indexed as

Chemotaxis, LeukocyteAnimalscdc42 GTP-Binding ProteinCell LineGene DeletionGene Knockdown TechniquesHumansInflammationMaleMiceMice, TransgenicMicrofilament ProteinsMyosin-Light-Chain PhosphataseNeutrophil InfiltrationNeutrophilsPhagocytosiscdc42 GTP-Binding ProteinMicrofilament ProteinsmoesinMyosin-Light-Chain Phosphataserac GTP-Binding Proteinsrho GTP-Binding ProteinsRho Guanine Nucleotide Exchange Factors

Identifiers

PMID25601651
PMCPMC4322047
OpenAlexW2157242572

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.