Evidence map›Paper›PMID 34106209›Full record

ArticleThe Journal of cell biology2021

MICAL2 enhances branched actin network disassembly by oxidizing Arp3B-containing Arp2/3 complexes.

Chiara Galloni, Davide Carra, Jasmine V G Abella, Svend Kjær, Pavithra Singaravelu, David J Barry, Naoko Kogata, Christophe Guérin, Laurent Blanchoin, Michael Way

Open access · hybridAbstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2021. 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
4.7field-weighted citation impact, top 4% 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, 50 citations in OpenAlex.

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  10. HIV-1 budding requires cortical actin disassembly by the oxidoreductase MICAL1.Proceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 3 countries.

Chiara Galloni *Cellular Signalling and Cytoskeletal Function Laboratory, The Francis Crick Institute, London, UK.
Davide Carra *Cellular Signalling and Cytoskeletal Function Laboratory, The Francis Crick Institute, London, UK.ORCID 0000-0003-0829-8668
Jasmine V G AbellaCellular Signalling and Cytoskeletal Function Laboratory, The Francis Crick Institute, London, UK.
Svend KjærStructural Biology Science Technology Platform, The Francis Crick Institute, London, UK.ORCID 0000-0001-9767-8683
Pavithra SingaraveluCytoMorpho Lab, Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, University of Grenoble-Alpes, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Grenoble, France.
David J BarryAdvanced Light Microscopy Facility, The Francis Crick Institute, London, UK.ORCID 0000-0003-2763-5244
Naoko KogataCellular Signalling and Cytoskeletal Function Laboratory, The Francis Crick Institute, London, UK.ORCID 0000-0002-7777-0797
Christophe GuérinCytoMorpho Lab, Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, University of Grenoble-Alpes, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Grenoble, France.
Laurent BlanchoinCytoMorpho Lab, Interdisciplinary Research Institute of Grenoble, Laboratoire de Physiologie Cellulaire & Végétale, University of Grenoble-Alpes, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Grenoble, France.ORCID 0000-0001-8146-9254
Michael WayCellular Signalling and Cytoskeletal Function Laboratory, The Francis Crick Institute, London, UK.ORCID 0000-0001-7207-2722
The Francis Crick Institute · GBCentre National de la Recherche Scientifique · FR

Funding

European Research Council 741773European Research Council 810207Medical Research Council FC001209Wellcome Trust
6 · The paper itself

Abstract

The mechanisms regulating the disassembly of branched actin networks formed by the Arp2/3 complex still remain to be fully elucidated. In addition, the impact of Arp3 isoforms on the properties of Arp2/3 are also unexplored. We now demonstrate that Arp3 and Arp3B isocomplexes promote actin assembly equally efficiently but generate branched actin networks with different disassembly rates. Arp3B dissociates significantly faster than Arp3 from the network, and its depletion increases actin stability. This difference is due to the oxidation of Arp3B, but not Arp3, by the methionine monooxygenase MICAL2, which is recruited to the actin network by coronin 1C. Substitution of Arp3B Met293 by threonine, the corresponding residue in Arp3, increases actin network stability. Conversely, replacing Arp3 Thr293 with glutamine to mimic Met oxidation promotes disassembly. The ability of MICAL2 to enhance network disassembly also depends on cortactin. Our observations demonstrate that coronin 1C, cortactin, and MICAL2 act together to promote disassembly of branched actin networks by oxidizing Arp3B-containing Arp2/3 complexes.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexActin-Related Protein 3CalponinsCortactinHeLa CellsHumansMicrofilament ProteinsMicroscopy, FluorescenceOxidation-ReductionOxidoreductasesVaccinia virusActin-Related Protein 2-3 ComplexActin-Related Protein 3ACTR3B protein, humanACTR3 protein, humanCalponinsCortactinCTTN protein, humanMICAL2 protein, humanMicrofilament ProteinsOxidoreductases

Identifiers

PMID34106209
PMCPMC8193582
OpenAlexW3169893861

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.