Evidence map›Paper›PMID 33495456›Full record

ArticleNature communications2021

A binding protein regulates myosin-7a dimerization and actin bundle assembly.

Rong Liu, Neil Billington, Yi Yang, Charles Bond, Amy Hong, Verl Siththanandan, Yasuharu Takagi, James R Sellers

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

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  9. The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025
    Article
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  20. Myosin motors in sensory hair bundle assembly.Current opinion in cell biology · 2022
    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

8 authors at 1 institution in 2 countries.

Rong LiuLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.ORCID 0000-0002-4062-0621
Neil BillingtonLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.ORCID 0000-0003-2306-0228
Yi YangLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.
Charles BondLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.
Amy HongLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.
Verl SiththanandanLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.ORCID 0000-0001-8005-4348
Yasuharu TakagiLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.
James R SellersLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA. Sellersj@nhlbi.nih.gov.ORCID 0000-0001-6296-564X
National Institutes of Health · US

Funding

Studies of Drosophila Myosin VIIZIAHL006049 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2010 to 2025
$9.7M
6 · The paper itself

Abstract

Myosin-7a, despite being monomeric in isolation, plays roles in organizing actin-based cell protrusions such as filopodia, microvilli and stereocilia, as well as transporting cargoes within them. Here, we identify a binding protein for Drosophila myosin-7a termed M7BP, and describe how M7BP assembles myosin-7a into a motile complex that enables cargo translocation and actin cytoskeletal remodeling. M7BP binds to the autoinhibitory tail of myosin-7a, extending the molecule and activating its ATPase activity. Single-molecule reconstitution show that M7BP enables robust motility by complexing with myosin-7a as 2:2 translocation dimers in an actin-regulated manner. Meanwhile, M7BP tethers actin, enhancing complex's processivity and driving actin-filament alignment during processive runs. Finally, we show that myosin-7a-M7BP complex assembles actin bundles and filopodia-like protrusions while migrating along them in living cells. Together, these findings provide insights into the mechanisms by which myosin-7a functions in actin protrusions.

Indexed as

Actin CytoskeletonActinsAnimalsCarrier ProteinsCell LineCell MovementDrosophila melanogasterDrosophila ProteinsMicroscopy, FluorescenceMultiprotein ComplexesMyosin VIIaProtein BindingProtein MultimerizationPseudopodiaStereociliaActinsCarrier ProteinsDrosophila ProteinsMultiprotein Complexesmyosin 7a, DrosophilaMyosin VIIa

Identifiers

PMID33495456
PMCPMC7835385
OpenAlexW3125253668

What OpenQuestion holds

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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.