Evidence map›Paper›PMID 17893244›Full record

ArticleThe Journal of cell biology2007

Myo4p is a monomeric myosin with motility uniquely adapted to transport mRNA.

Brian D Dunn, Takeshi Sakamoto, Myoung-Soon S Hong, James R Sellers, Peter A Takizawa

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

37 citing papers in PubMed, 52 citations in OpenAlex.

  1. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  2. Article
  3. Article
  4. Article
  5. Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  6. Flexural Stiffness of Myosin Va Subdomains as Measured from Tethered Particle Motion.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2015
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Principles of mRNA transport in yeast.Cellular and molecular life sciences : CMLS · 2012
    Review
  18. Control of cytoplasmic mRNA localization.Cellular and molecular life sciences : CMLS · 2012
    Review
  19. Plant-Specific Myosin XI, a Molecular Perspective.Frontiers in plant science · 2012
    Article
  20. Structural and functional insights on the Myosin superfamily.Bioinformatics and biology insights · 2012
    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

5 authors at 2 institutions in 1 country.

Brian D DunnDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA.
Takeshi Sakamoto
Myoung-Soon S Hong
James R Sellers
Peter A Takizawa
Yale University · USNational Institutes of Health · US

Funding

Mechanism of mRNA transport by Myo4pR01GM073734 · NIGMS · YALE UNIVERSITY · PI TAKIZAWA, PETER A · 2005 to 2009
$1.3M
Studies Of Myosin VZ01HL004229 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES R. · 1997 to 2008
$1.1M
NIGMS NIH HHS GM073734NIGMS NIH HHS R01 GM073734
6 · The paper itself

Abstract

The yeast Saccharomyces cerevisiae uses two class V myosins to transport cellular material into the bud: Myo2p moves secretory vesicles and organelles, whereas Myo4p transports mRNA. To understand how Myo2p and Myo4p are adapted to transport physically distinct cargos, we characterize Myo2p and Myo4p in yeast extracts, purify active Myo2p and Myo4p from yeast lysates, and analyze their motility. We find several striking differences between Myo2p and Myo4p. First, Myo2p forms a dimer, whereas Myo4p is a monomer. Second, Myo4p generates higher actin filament velocity at lower motor density. Third, single molecules of Myo2p are weakly processive, whereas individual Myo4p motors are nonprocessive. Finally, Myo4p self-assembles into multi-motor complexes capable of processive motility. We show that the unique motility of Myo4p is not due to its motor domain and that the motor domain of Myo2p can transport ASH1 mRNA in vivo. Our results suggest that the oligomeric state of Myo4p is important for its motility and ability to transport mRNA.

Indexed as

RNA TransportCross-Linking ReagentsEthyldimethylaminopropyl CarbodiimideGreen Fluorescent ProteinsMicroscopy, ElectronMolecular Motor ProteinsMyosin Heavy ChainsMyosinsMyosin Type VProtein Structure, QuaternaryProtein Structure, TertiaryProtein TransportRecombinant Fusion ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCross-Linking ReagentsEthyldimethylaminopropyl CarbodiimideGreen Fluorescent ProteinsMolecular Motor ProteinsMYO2 protein, S cerevisiaeMyo4 protein, S cerevisiaeMyosin Heavy ChainsMyosinsMyosin Type VRecombinant Fusion ProteinsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID17893244
PMCPMC2064653
OpenAlexW2121869607

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.