Evidence map›Paper›PMID 27623148›Full record

ArticleeLife2016

Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes.

Olena Pylypenko, Tobias Welz, Janine Tittel, Martin Kollmar, Florian Chardon, Gilles Malherbe, Sabine Weiss, Carina Ida Luise Michel, Annette Samol-Wolf, Andreas Till Grasskamp and 9 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.7field-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

35 citing papers in PubMed, 70 citations in OpenAlex.

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  11. mBio · 2023
    Article
  12. Article
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  14. Article
  15. Review
  16. Article
  17. Spire1 and Myosin Vc promote CaCellular and molecular life sciences : CMLS · 2022
    Article
  18. Review
  19. Article
  20. Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021
    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

19 authors at 6 institutions in 4 countries.

Olena PylypenkoInstitut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Tobias WelzUniversity Hospital Regensburg, Regensburg, Germany.
Janine TittelMax Planck Institute of Biochemistry, Martinsried, Germany.
Martin KollmarMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Florian ChardonInstitut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Gilles MalherbeInstitut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Sabine WeissUniversity Hospital Regensburg, Regensburg, Germany.
Carina Ida Luise MichelUniversity Hospital Regensburg, Regensburg, Germany.
Annette Samol-WolfUniversity Hospital Regensburg, Regensburg, Germany.
Andreas Till GrasskampUniversity Hospital Regensburg, Regensburg, Germany.ORCID 0000-0002-5895-6529
Alistair HumeUniversity of Nottingham, Nottingham, United Kingdom.
Bruno GoudInstitut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Bruno BaronInstitut Pasteur, Biophysics of Macromolecules and their Interactions, Paris, France.
Patrick EnglandInstitut Pasteur, Biophysics of Macromolecules and their Interactions, Paris, France.
Margaret A TitusDepartment of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, United States.
Petra SchwilleMax Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-6106-4847
Thomas WeidemannMax Planck Institute of Biochemistry, Martinsried, Germany.
Anne HoudusseInstitut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Eugen KerkhoffUniversity Hospital Regensburg, Regensburg, Germany.ORCID 0000-0002-3640-7916
Centre National de la Recherche Scientifique · FRUniversity Hospital Regensburg · DEMax Planck Institute of Biochemistry · DEMax Planck Institute for Biophysical Chemistry · DEUniversity of Minnesota · USUniversity of Nottingham · GB

Funding

Medical Research Council G1100063
6 · The paper itself

Abstract

There is growing evidence for a coupling of actin assembly and myosin motor activity in cells. However, mechanisms for recruitment of actin nucleators and motors on specific membrane compartments remain unclear. Here we report how Spir actin nucleators and myosin V motors coordinate their specific membrane recruitment. The myosin V globular tail domain (MyoV-GTD) interacts directly with an evolutionarily conserved Spir sequence motif. We determined crystal structures of MyoVa-GTD bound either to the Spir-2 motif or to Rab11 and show that a Spir-2:MyoVa:Rab11 complex can form. The ternary complex architecture explains how Rab11 vesicles support coordinated F-actin nucleation and myosin force generation for vesicle transport and tethering. New insights are also provided into how myosin activation can be coupled with the generation of actin tracks. Since MyoV binds several Rab GTPases, synchronized nucleator and motor targeting could provide a common mechanism to control force generation and motility in different cellular processes.

Indexed as

AnimalsCrystallography, X-RayCytoplasmic VesiclesMembranesMiceMicrofilament ProteinsModels, MolecularMyosin Type VProtein BindingProtein ConformationProtein Multimerizationrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsMicrofilament ProteinsMyosin Type Vrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsSpir-2 protein, mouseactin motor proteinsactin nucleationbiophysicscell biologymyosin VnoneRab11Spirestructural biologyvesicle transport

Identifiers

PMID27623148
PMCPMC5021521
OpenAlexW2519817583

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.