Evidence map›Paper›PMID 21289089›Full record

ArticleMolecular biology of the cell2011

CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation.

J L Cannon, P D Mody, K M Blaine, E J Chen, A D Nelson, L J Sayles, T V Moore, B S Clay, N O Dulin, R A Shilling and 2 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. The Impact of Zinc on T Cell Motility and the Immunological Synapse.International journal of molecular sciences · 2026
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  13. Buprenorphine decreases the CCL2-mediated chemotactic response of monocytes.Journal of immunology (Baltimore, Md. : 1950) · 2015
    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

12 authors at 3 institutions in 2 countries.

J L CannonSection of Pulmonary and Critical Care Medicine, Department of Medicine, University of Chicago, Chicago, IL 60637, USA. jucannon@salud.unm.edu
P D Mody
K M Blaine
E J Chen
A D Nelson
L J Sayles
T V Moore
B S Clay
N O Dulin
R A Shilling
J K Burkhardt
A I Sperling
University of New Mexico · USUniversity of Chicago · USChildren's Hospital of Philadelphia · US

Funding

CD43 REGULATION OF IMMUNE RESPONSESR01AI044932 · NIAID · UNIVERSITY OF CHICAGO · PI SPERLING, ANNE I. · 2000 to 2010
$3.1M
Activation of protein kinase A by endothelin-1R01HL071755 · NHLBI · UNIVERSITY OF CHICAGO · PI DULIN, NICKOLAI O · 2005 to 2009
$1.5M
NHLBI NIH HHS R01 HL071755NHLBI NIH HHS R01 HL-71755NIAID NIH HHS R01 AI-044932NIAID NIH HHS R01 AI044932
6 · The paper itself

Abstract

Cell polarization is a key feature of cell motility, driving cell migration to tissues. CD43 is an abundantly expressed molecule on the T-cell surface that shows distinct localization to the migrating T-cell uropod and the distal pole complex (DPC) opposite the immunological synapse via association with the ezrin-radixin-moesin (ERM) family of actin regulatory proteins. CD43 regulates multiple T-cell functions, including T-cell activation, proliferation, apoptosis, and migration. We recently demonstrated that CD43 regulates T-cell trafficking through a phosphorylation site at Ser-76 (S76) within its cytoplasmic tail. Using a phosphorylation-specific antibody, we now find that CD43 phosphorylation at S76 is enhanced by migration signals. We further show that CD43 phosphorylation and normal T-cell trafficking depend on CD43 association with ERM proteins. Interestingly, mutation of S76 to mimic phosphorylation enhances T-cell migration and CD43 movement to the DPC while blocking ERM association, showing that CD43 movement can occur in the absence of ERM binding. We also find that protein kinase CΘ can phosphorylate CD43. These results show that while CD43 binding to ERM proteins is crucial for S76 phosphorylation, CD43 movement and regulation of T-cell migration can occur through an ERM-independent, phosphorylation-dependent mechanism.

Indexed as

AnimalsCell MovementCells, CulturedCytoskeletal ProteinsEzrinImmunological SynapsesIsoenzymesLeukosialinMembrane ProteinsMiceMice, TransgenicMicrofilament ProteinsProtein Kinase CProtein Kinase C-thetaRecombinant Fusion ProteinsT-LymphocytesCytoskeletal ProteinsEzrinIsoenzymesLeukosialinMembrane ProteinsMicrofilament ProteinsmoesinPrkcq protein, mouseProtein Kinase CProtein Kinase C-thetaradixinRecombinant Fusion Proteins

Identifiers

PMID21289089
PMCPMC3069020
OpenAlexW2164855090

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.