Evidence map›Paper›PMID 14565972›Full record

ArticleMolecular biology of the cell2004

Myosin-Va binds to and mechanochemically couples microtubules to actin filaments.

Tracy T Cao, Wakam Chang, Sarah E Masters, Mark S Mooseker

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

24 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Review
  3. Roles of Myosin-Mediated Membrane Trafficking in TGF-β Signaling.International journal of molecular sciences · 2019
    Review
  4. Defects in Axonal Transport in Inherited Neuropathies.Journal of neuromuscular diseases · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Myosin V and Kinesin act as tethers to enhance each others' processivity.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  19. Slip sliding away with myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  20. Myosin Va maneuvers through actin intersections and diffuses along microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

4 authors at 1 institution in 1 country.

Tracy T CaoDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA.
Wakam Chang
Sarah E Masters
Mark S Mooseker
Yale University · US

Funding

UNCONVENTIONAL MYOSINS IN RENAL FUNCTIONSP01DK055389 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1999 to 2004
$4.9M
Myosin Functions in the EnterocyteR01DK025387 · NIDDK · YALE UNIVERSITY · PI MOOSEKER, MARK S · 1986 to 2010
$3.6M
Myosin Functions in the EnterocyteR56DK025387 · NIDDK · YALE UNIVERSITY · PI MOOSEKER, MARK S · 2012 to 2012
$360k
CYTOSKELETAL STRUCTURE OF THE INTESTINAL BRUSH BORDERR37DK025387 · NIDDK · YALE UNIVERSITY · PI MOOSEKER, MARK S · 1992 to 1999
–
NIDDK NIH HHS DK 25387NIDDK NIH HHS DK 55389NIDDK NIH HHS P01 DK055389NIDDK NIH HHS R01 DK025387NIDDK NIH HHS R37 DK025387NIDDK NIH HHS R56 DK025387
6 · The paper itself

Abstract

Myosin-Va was identified as a microtubule binding protein by cosedimentation analysis in the presence of microtubules. Native myosin-Va purified from chick brain, as well as the expressed globular tail domain of this myosin, but not head domain bound to microtubule-associated protein-free microtubules. Binding of myosin-Va to microtubules was saturable and of moderately high affinity (approximately 1:24 Myosin-Va:tubulin; Kd = 70 nM). Myosin-Va may bind to microtubules via its tail domain because microtubule-bound myosin-Va retained the ability to bind actin filaments resulting in the formation of cross-linked gels of microtubules and actin, as assessed by fluorescence and electron microscopy. In low Ca2+, ATP addition induced dissolution of these gels, but not release of myosin-Va from MTs. However, in 10 microM Ca2+, ATP addition resulted in the contraction of the gels into aster-like arrays. These results demonstrate that myosin-Va is a microtubule binding protein that cross-links and mechanochemically couples microtubules to actin filaments.

Indexed as

Actin CytoskeletonAdenosine TriphosphateAnimalsBrainCalciumCells, CulturedChickensInsectaMicroscopy, ElectronMicroscopy, FluorescenceMicrotubulesMuscle ContractionMyosin Heavy ChainsMyosin Type VProtein BindingProtein Structure, TertiaryAdenosine TriphosphateCalciumMyosin Heavy ChainsMyosin Type V

Identifiers

PMID14565972
PMCPMC307536
OpenAlexW2135292982

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.