Evidence map›Paper›PMID 21339367›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2011

Conformational switching in ezrin regulates morphological and cytoskeletal changes required for B cell chemotaxis.

Neetha Parameswaran, Ken Matsui, Neetu Gupta

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 43 citations in OpenAlex.

  1. Inherited human ezrin deficiency impairs adaptive immunity.The Journal of allergy and clinical immunology · 2023
    Article
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  3. Article
  4. Review
  5. Article
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  11. Article
  12. Article
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  14. Review
  15. Article
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  18. Cutting Edge: Ezrin Regulates Inflammation by Limiting B Cell IL-10 Production.Journal of immunology (Baltimore, Md. : 1950) · 2016
    Article
  19. Article
  20. Review
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

3 authors at 1 institution in 1 country.

Neetha ParameswaranDepartment of Immunology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Ken Matsui
Neetu Gupta
Cleveland Clinic Lerner College of Medicine · US

Funding

Regulation of B Cell Function by Membrane-Cytoskeletal RemodelingR01AI081743 · NIAID · CLEVELAND CLINIC LERNER COM-CWRU · PI GUPTA, NEETU · 2009 to 2012
$1.5M
Regulation of B Cell Function by Membrane-Cytoskeletal RemodelingR56AI081743 · NIAID · CLEVELAND CLINIC LERNER COM-CWRU · PI GUPTA, NEETU · 2014 to 2014
$383k
NIAID NIH HHS AI081743NIAID NIH HHS R01 AI081743NIAID NIH HHS R56 AI081743NIDDK NIH HHS DK068242
6 · The paper itself

Abstract

B cell chemotaxis occurs in response to specific chemokine gradients and is critical for homeostasis and immune response. The molecular regulation of B cell membrane-actin interactions during migration is poorly understood. In this study, we report a role for ezrin, a member of the membrane-cytoskeleton cross-linking ezrin-radixin-moesin proteins, in the regulation of the earliest steps of B cell polarization and chemotaxis. We visualized chemokine-induced changes in murine B cell morphology using scanning electron microscopy and spatiotemporal dynamics of ezrin in B cells using epifluorescence and total internal reflection microscopy. Upon chemokine stimulation, ezrin is transiently dephosphorylated to assume an inactive conformation and localizes to the lamellipodia. B cells expressing a phosphomimetic conformationally active mutant of ezrin or those in which ezrin dephosphorylation was pharmacologically inhibited displayed impaired microvillar dynamics, morphological polarization, and chemotaxis. Our data suggest a 2-fold involvement of ezrin in B cell migration, whereby it first undergoes chemokine-induced dephosphorylation to facilitate membrane flexibility, followed by relocalization to the actin-rich lamellipodia for dynamic forward protrusion of the cells.

Indexed as

ActinsAmino Acid SubstitutionAnimalsB-Lymphocyte SubsetsCell Line, TumorCell Migration InhibitionChemotaxis, LeukocyteCytoskeletal ProteinsCytoskeletonEzrinMiceMice, Inbred C57BLMicrofilament ProteinsMutagenesis, Site-DirectedPhosphorylationProtein ConformationActinsCytoskeletal ProteinsEzrinMicrofilament ProteinsmoesinThreonine

Identifiers

PMID21339367
PMCPMC3106416
OpenAlexW1912844437

What OpenQuestion holds

Textmetadata
LicenceTDM
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.