Evidence map›Paper›PMID 22084309›Full record

ArticleThe Journal of cell biology2011

Two single-headed myosin V motors bound to a tetrameric adapter protein form a processive complex.

Elena B Krementsova, Alex R Hodges, Carol S Bookwalter, Thomas E Sladewski, Mirko Travaglia, H Lee Sweeney, Kathleen M Trybus

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. 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
  8. Article
  9. Article
  10. Structural insights into the assembly of a monomeric class V myosin.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Structure of a myosin•adaptor complex and pairing by cargo.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Principles of mRNA transport in yeast.Cellular and molecular life sciences : CMLS · 2012
    Review
  19. Review
  20. Plant-Specific Myosin XI, a Molecular Perspective.Frontiers in plant science · 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

7 authors at 2 institutions in 1 country.

Elena B KrementsovaDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA.
Alex R Hodges
Carol S Bookwalter
Thomas E Sladewski
Mirko Travaglia
H Lee Sweeney
Kathleen M Trybus
University of Vermont · USUniversity of Pennsylvania · US

Funding

MUTATIONAL STUDIES OF PROCESSIVE MYOSIN MOTORSR01GM078097 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 2007 to 2019
$4.8M
PHYSIOLOGY AND MYOSIN ISOZYMES OF SKELETAL MUSCLE FIBERSR01AR035661 · NIAMS · UNIVERSITY OF TEXAS AUSTIN · PI SWEENEY, H LEE · 1986 to 2010
$3.7M
NIAMS NIH HHS AR35661NIAMS NIH HHS R01 AR035661NIGMS NIH HHS GM078097NIGMS NIH HHS R01 GM078097
6 · The paper itself

Abstract

Myo4p, one of two class V myosins in budding yeast, continuously transports messenger RNA (mRNA) cargo in the cell but is nonprocessive when characterized in vitro. The adapter protein She3p tightly binds to the Myo4p rod, forming a single-headed motor complex. In this paper, we show that two Myo4p-She3p motors are recruited by the tetrameric mRNA-binding protein She2p to form a processive double-headed complex. The binding site for She3p was mapped to a single α helix that protrudes at right angles from She2p. Processive runs of several micrometers on yeast actin-tropomyosin filaments were observed only in the presence of She2p, and, thus, motor activity is regulated by cargo binding. While moving processively, each head steps ~72 nm in a hand-over-hand motion. Coupling two high-duty cycle monomeric motors via a common cargo-binding adapter protein creates a complex with transport properties comparable with a single dimeric processive motor such as vertebrate myosin Va.

Indexed as

Models, MolecularMyosin Heavy ChainsMyosin Type VProtein ConformationRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMyo4 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type VRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSHE2 protein, S cerevisiaeSHE3 protein, S cerevisiae

Identifiers

PMID22084309
PMCPMC3257522
OpenAlexW2142298504

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.