Evidence map›Paper›PMID 15007063›Full record

ArticleThe Journal of cell biology2004

Myosin V: regulation by calcium, calmodulin, and the tail domain.

Dimitry N Krementsov, Elena B Krementsova, Kathleen M Trybus

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 209 citations in OpenAlex.

  1. Article
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  5. Myosin-5 varies its step length to carry cargo straight along the irregular F-actin track.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Myosin-5 varies its steps along the irregular F-actin track.bioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020
    Review
  16. Journal of cell science · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. Article

51 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Dimitry N KrementsovDept. of Molecular Physiology and Biophysics, University of Vermont, 130 Health Science Research Facility, Burlington, VT 05405-0068, USA.
Elena B Krementsova
Kathleen M Trybus
University of Vermont · US

Funding

SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
NHLBI NIH HHS HL38113NHLBI NIH HHS R01 HL038113
6 · The paper itself

Abstract

Calcium activates the ATPase activity of tissue-purified myosin V, but not that of shorter expressed constructs. Here, we resolve this discrepancy by comparing an expressed full-length myosin V (dFull) to three shorter constructs. Only dFull has low ATPase activity in EGTA, and significantly higher activity in calcium. Based on hydrodynamic data and electron microscopic images, the inhibited state is due to a compact conformation that is possible only with the whole molecule. The paradoxical finding that dFull moved actin in EGTA suggests that binding of the molecule to the substratum turns it on, perhaps mimicking cargo activation. Calcium slows, but does not stop the rate of actin movement if excess calmodulin (CaM) is present. Without excess CaM, calcium binding to the high affinity sites dissociates CaM and stops motility. We propose that a folded-to-extended conformational change that is controlled by calcium and CaM, and probably by cargo binding itself, regulates myosin V's ability to transport cargo in the cell.

Indexed as

Protein ConformationActinsAdenosine TriphosphatasesAnimalsBinding SitesCalciumCalmodulinChelating AgentsEgtazic AcidHumansMiceModels, MolecularMolecular Motor ProteinsMyosin Type VProtein Structure, TertiarySaltsActinsAdenosine TriphosphatasesCalciumCalmodulinChelating AgentsEgtazic AcidMolecular Motor ProteinsMyosin Type VSalts

Identifiers

PMID15007063
PMCPMC2172279
OpenAlexW2013539793

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.