Evidence map›Paper›PMID 33941653›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2021

MYO1F Regulates IgE and MRGPRX2-Dependent Mast Cell Exocytosis.

Arnau Navinés-Ferrer, Erola Ainsua-Enrich, Eva Serrano-Candelas, Elizabeth Proaño-Pérez, Rosa Muñoz-Cano, Gabriel Gastaminza, Ana Olivera, Margarita Martin

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 27% 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, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Potential Role of Moesin in Regulating Mast Cell Secretion.International journal of molecular sciences · 2023
    Review
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  6. Article
  7. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 4 countries.

Arnau Navinés-FerrerBiochemistry Unit, Biomedicine Department, University of Barcelona, Barcelona, Spain.ORCID 0000-0002-3806-4021
Erola Ainsua-EnrichBiochemistry Unit, Biomedicine Department, University of Barcelona, Barcelona, Spain.
Eva Serrano-CandelasBiochemistry Unit, Biomedicine Department, University of Barcelona, Barcelona, Spain.ORCID 0000-0002-8929-5364
Elizabeth Proaño-PérezBiochemistry Unit, Biomedicine Department, University of Barcelona, Barcelona, Spain.
Rosa Muñoz-CanoLaboratory of Clinic and Experimental Respiratory Immunoallergy, August Pi i Sunyer Biomedical Research Institute, Barcelona, Spain.ORCID 0000-0001-8566-8285
Gabriel GastaminzaAsthma, Adverse Drug Reactions and Allergy Research Network (ARADyAL), Spain.ORCID 0000-0001-6325-3847
Ana OliveraMast Cell Biology Section, Laboratory of Allergic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD.ORCID 0000-0002-0128-5461
Margarita MartinBiochemistry Unit, Biomedicine Department, University of Barcelona, Barcelona, Spain martin_andorra@ub.edu.ORCID 0000-0002-9245-4899
Institute for Research in Biomedicine · ESSpanish Clinical Research Network · ESNational Institutes of Health · US

Funding

Identification and Characterization of Signaling Pathways and Mediators Regulating Mast Cell-Related DisordersZIAAI001206 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI OLIVERA, ANA · 2015 to 2025
$11.3M
Intramural NIH HHS ZIA AI001206
6 · The paper itself

Abstract

The activation and degranulation of mast cells is critical in the pathogenesis of allergic inflammation and modulation of inflammation. Recently, we demonstrated that the unconventional long-tailed myosin, MYO1F, localizes with cortical F-actin and mediates adhesion and migration of mast cells. In this study, we show that knockdown of MYO1F by short hairpin RNA reduces human mast cell degranulation induced by both IgE crosslinking and by stimulation of the Mas-related G protein-coupled receptor X2 (MRGPRX2), which has been associated with allergic and pseudoallergic drug reactions, respectively. Defective degranulation was accompanied by a reduced reassembly of the cortical actin ring after activation but reversed by inhibition of actin polymerization. Our data show that MYO1F is required for full Cdc42 GTPase activation, a critical step in exocytosis. Furthermore, MYO1F knockdown resulted in less granule localization in the cell membrane and fewer fissioned mitochondria along with deficient mitochondria translocation to exocytic sites. Consistent with that, AKT and DRP1 phosphorylation are diminished in MYO1F knockdown cells. Altogether, our data point to MYO1F as an important regulator of mast cell degranulation by contributing to the dynamics of the cortical actin ring and the distribution of both the secretory granules and mitochondria.

Indexed as

Actin CytoskeletonActinsBlood DonorsCell DegranulationGene Knockdown TechniquesHEK293 CellsHumansImmunoglobulin EMast CellsMitochondriaMyosin Type INerve Tissue ProteinsPolymerizationReceptors, G-Protein-CoupledReceptors, NeuropeptideSecretory VesiclesActinsImmunoglobulin EMRGPRX2 protein, humanMYO1F protein, humanMyosin Type INerve Tissue ProteinsReceptors, G-Protein-CoupledReceptors, Neuropeptide

Identifiers

PMID33941653
PMCPMC8113095
OpenAlexW3158705058

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.