Evidence map›Paper›PMID 24248336›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structural basis of myosin V Rab GTPase-dependent cargo recognition.

Olena Pylypenko, Wikayatou Attanda, Charles Gauquelin, Marion Lahmani, Doudouh Coulibaly, Bruno Baron, Sylviane Hoos, Margaret A Titus, Patrick England, Anne M Houdusse

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.3field-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

47 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
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  6. Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System.International journal of molecular sciences · 2023
    Review
  7. Article
  8. A Novel Constitutively ActiveHuman mutation · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  13. Article
  14. Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021
    Review
  15. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  16. Article
  17. Article
  18. Article
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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

10 authors at 3 institutions in 4 countries.

Olena PylypenkoStructural Motility, Institut Curie, 75248 Paris Cedex 05, France.
Wikayatou Attanda
Charles Gauquelin
Marion Lahmani
Doudouh Coulibaly
Bruno Baron
Sylviane Hoos
Margaret A Titus
Patrick England
Anne M Houdusse
Centre National pour la Recherche Scientifique et Technique (CNRST) · MAInstitut Pasteur · FRUniversity of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specific recognition of the cargo that molecular motors transport or tether to cytoskeleton tracks allows them to perform precise cellular functions at particular times and positions in cells. However, very little is known about how evolution has favored conservation of functions for some isoforms, while also allowing for the generation of new recognition sites and specialized cellular functions. Here we present several crystal structures of the myosin Va or the myosin Vb globular tail domain (GTD) that gives insights into how the motor is linked to the recycling membrane compartments via Rab11 or to the melanosome membrane via recognition of the melanophilin adaptor that binds to Rab27a. The structures illustrate how the Rab11-binding site has been conserved during evolution and how divergence at another site of the GTD allows more specific interactions such as the specific recognition of melanophilin by the myosin Va isoform. With atomic structural insights, these structures also show how either the partner or the GTD structural plasticity upon association is critical for selective recruitment of the motor.

Indexed as

Adaptor Proteins, Signal TransducingCrystallography, X-RayHumansIntracellular MembranesMelanosomesMyosin Heavy ChainsMyosin Type VProtein Structure, QuaternaryProtein Structure, Tertiaryrab11 GTP-Binding Proteinsrab27 GTP-Binding Proteinsrab GTP-Binding ProteinsAdaptor Proteins, Signal TransducingMLPH protein, humanMYO5A protein, humanMYO5B protein, humanMyosin Heavy ChainsMyosin Type Vrab11 GTP-Binding ProteinsRAB27A protein, humanrab27 GTP-Binding Proteinsrab GTP-Binding ProteinsDIL motifGTPasesintracellular trafficRab effector

Identifiers

PMID24248336
PMCPMC3870677
OpenAlexW2080400460

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.