Evidence map›Paper›PMID 32661131›Full record

ArticleBiology open2020

Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms.

Ottilie von Loeffelholz, Andrew Purkiss, Luyan Cao, Svend Kjaer, Naoko Kogata, Guillaume Romet-Lemonne, Michael Way, Carolyn A Moores

Open access · goldAbstract read
In one paragraph

Article in Biology open, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.8field-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

19 citing papers in PubMed, 26 citations in OpenAlex.

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  12. Initial ciliary assembly inMolecular biology of the cell · 2023
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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

8 authors at 4 institutions in 2 countries.

Ottilie von LoeffelholzDepartment of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.
Andrew PurkissThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Luyan CaoUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
Svend KjaerThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Naoko KogataThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Guillaume Romet-LemonneUniversité de Paris, CNRS, Institut Jacques Monod, 75013 Paris, France.
Michael WayThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK michael.way@crick.ac.uk c.moores@mail.cryst.bbk.ac.uk.ORCID 0000-0001-7207-2722
Carolyn A MooresDepartment of Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK michael.way@crick.ac.uk c.moores@mail.cryst.bbk.ac.uk.ORCID 0000-0001-5686-6290
The Francis Crick Institute · GBCentre National de la Recherche Scientifique · FRInstitut de génétique et de biologie moléculaire et cellulaire · FRInstitute of Structural and Molecular Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L00190X/1European Research Council 810207Medical Research Council FC001209Wellcome Trust FC001209
6 · The paper itself

Abstract

The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce a family of Arp2/3 complexes with different properties that may be suited to different physiological contexts. To shed light on how isoform diversification affects Arp2/3 function, we determined a 4.2 Å resolution cryo-EM structure of the most active human Arp2/3 complex containing ARPC1B and ARPC5L, and compared it with the structure of the least active ARPC1A-ARPC5-containing complex. The architecture of each isoform-specific Arp2/3 complex is the same. Strikingly, however, the N-terminal half of ARPC5L is partially disordered compared to ARPC5, suggesting that this region of ARPC5/ARPC5L is an important determinant of complex activity. Confirming this idea, the nucleation activity of Arp2/3 complexes containing hybrid ARPC5/ARPC5L subunits is higher when the ARPC5L N-terminus is present, thereby providing insight into activity differences between the different Arp2/3 complexes.

Indexed as

Cryoelectron MicroscopyActin CytoskeletonActin-Related Protein 2-3 ComplexActinsHumansModels, MolecularMutationProtein BindingProtein ConformationStructure-Activity RelationshipActin-Related Protein 2-3 ComplexActinsARPC5 protein, humanActinArp2/3Cryo-EMCytoskeletonIsoformsNucleation

Identifiers

PMID32661131
PMCPMC7406314
OpenAlexW3040954773

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.