Evidence map›Paper›PMID 31744880›Full record

ArticleThe Journal of biological chemistry2020

Competition between two high- and low-affinity protein-binding sites in myosin VI controls its cellular function.

Natalia Fili, Yukti Hari-Gupta, Bjork Aston, Ália Dos Santos, Rosemarie E Gough, Bana Alamad, Lin Wang, Marisa L Martin-Fernandez, Christopher P Toseland

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Cardiolipin membranes drive Myosin VI activation, oligomerization, and processive cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Myosin in chromosome organisation and gene expression.Biochemical Society transactions · 2023
    Review
  7. Article
  8. Disabled-2 (International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Regulation of Nuclear Mechanics and the Impact on DNA Damage.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  15. Article
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

9 authors at 3 institutions in 1 country.

Natalia FiliSheffield Cancer Centre, Department of Oncology and Metabolism, University of Sheffield, Sheffield S10 2RX, United Kingdom.
Yukti Hari-GuptaSchool of Biosciences, University of Kent, Canterbury CT2 7NZ, United Kingdom.
Bjork AstonSchool of Biosciences, University of Kent, Canterbury CT2 7NZ, United Kingdom.
Ália Dos SantosSheffield Cancer Centre, Department of Oncology and Metabolism, University of Sheffield, Sheffield S10 2RX, United Kingdom.
Rosemarie E GoughSheffield Cancer Centre, Department of Oncology and Metabolism, University of Sheffield, Sheffield S10 2RX, United Kingdom.
Bana AlamadSchool of Biosciences, University of Kent, Canterbury CT2 7NZ, United Kingdom.
Lin WangCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell, Didcot, Oxford OX11 0QX, United Kingdom.
Marisa L Martin-FernandezCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell, Didcot, Oxford OX11 0QX, United Kingdom.
Christopher P ToselandSheffield Cancer Centre, Department of Oncology and Metabolism, University of Sheffield, Sheffield S10 2RX, United Kingdom. Electronic address: c.toseland@sheffield.ac.uk.
University of Sheffield · GBUniversity of Kent · GBRutherford Appleton Laboratory · GB

Funding

Medical Research Council MC_EX_MR/K015591/1Medical Research Council MR/M020606/1Medical Research Council MR/M020606/2
6 · The paper itself

Abstract

Myosin VI is involved in many cellular processes ranging from endocytosis to transcription. This multifunctional potential is achieved through alternative isoform splicing and through interactions of myosin VI with a diverse network of binding partners. However, the interplay between these two modes of regulation remains unexplored. To this end, we compared two different binding partners and their interactions with myosin VI by exploring the kinetic properties of recombinant proteins and their distribution in mammalian cells using fluorescence imaging. We found that selectivity for these binding partners is achieved through a high-affinity motif and a low-affinity motif within myosin VI. These two motifs allow competition among partners for myosin VI. Exploring how this competition affects the activity of nuclear myosin VI, we demonstrate the impact of a concentration-driven interaction with the low-affinity binding partner DAB2, finding that this interaction blocks the ability of nuclear myosin VI to bind DNA and its transcriptional activity

Indexed as

Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBinding SitesCell NucleusHeLa CellsHumansMCF-7 CellsMyosin Heavy ChainsProtein BindingProtein Interaction MapsProtein MultimerizationAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsDAB2 protein, humanMyosin Heavy Chainsmyosin VIbiophysicsgene expressiongene regulationkineticsmyosin

Identifiers

PMID31744880
PMCPMC6956527
OpenAlexW2990459127

What OpenQuestion holds

Textmetadata
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.