Evidence map›Paper›PMID 17683200›Full record

ArticlePLoS biology2007

Precise positioning of myosin VI on endocytic vesicles in vivo.

David Altman, Debanjan Goswami, Tama Hasson, James A Spudich, Satyajit Mayor

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.8field-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

26 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Unconventional Myosins fromBiomolecules · 2022
    Review
  5. Article
  6. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  7. Article
  8. Article
  9. Filopodia formation and endosome clustering induced by mutant plus-end-directed myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Fluorescent labeling and modification of proteins.Journal of chemical biology · 2013
    Review
  12. Article
  13. Article
  14. Review
  15. Principles of unconventional myosin function and targeting.Annual review of cell and developmental biology · 2011
    Review
  16. Article
  17. Review
  18. Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  19. Review
  20. 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 3 institutions in 2 countries.

David AltmanDepartment of Biochemistry, Stanford University Medical Center, Stanford, California, United States of America.
Debanjan Goswami
Tama Hasson
James A Spudich
Satyajit Mayor
National Centre for Biological Sciences · INStanford Medicine · USUniversity of California, San Diego · US

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
NIGMS NIH HHS GM33289NIGMS NIH HHS R01 GM033289Wellcome TrustWellcome Trust 056727/Z/99
6 · The paper itself

Abstract

Myosin VI has been studied in both a monomeric and a dimeric form in vitro. Because the functional characteristics of the motor are dramatically different for these two forms, it is important to understand whether myosin VI heavy chains are brought together on endocytic vesicles. We have used fluorescence anisotropy measurements to detect fluorescence resonance energy transfer between identical fluorophores (homoFRET) resulting from myosin VI heavy chains being brought into close proximity. We observed that, when associated with clathrin-mediated endocytic vesicles, myosin VI heavy chains are precisely positioned to bring their tail domains in close proximity. Our data show that on endocytic vesicles, myosin VI heavy chains are brought together in an orientation that previous in vitro studies have shown causes dimerization of the motor. Our results are therefore consistent with vesicle-associated myosin VI existing as a processive dimer, capable of its known trafficking function.

Indexed as

Protein Structure, QuaternaryAnimalsAnisotropyCell LineDimerizationEndocytosisFluorescent DyesHumansMyosin Heavy ChainsRecombinant Fusion ProteinsTransferrinTransport VesiclesFluorescent DyesMyosin Heavy Chainsmyosin VIRecombinant Fusion ProteinsTransferrin

Identifiers

PMID17683200
PMCPMC1939883
OpenAlexW2074139652

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.