Evidence map›Paper›PMID 20538589›Full record

ArticleThe Journal of biological chemistry2010

Head of myosin IX binds calmodulin and moves processively toward the plus-end of actin filaments.

Wanqin Liao, Kerstin Elfrink, Martin Bähler

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Unconventional Myosins fromBiomolecules · 2022
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Self-organization of actin networks by a monomeric myosin.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppression.The Journal of clinical investigation · 2015
    Article
  20. Association between the MYO9B polymorphisms and celiac disease risk: a meta-analysis.International journal of clinical and experimental medicine · 2015
    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

3 authors.

Wanqin LiaoInstitute of Molecular Cell Biology, Westfalian Wilhelms-University, 48149 Münster, Germany.
Kerstin Elfrink
Martin Bähler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian myosin IXb (Myo9b) has been shown to exhibit unique motor properties in that it is a single-headed processive motor and the rate-limiting step in its chemical cycle is ATP hydrolysis. Furthermore, it has been reported to move toward the minus- and the plus-end of actin filaments. To analyze the contribution of the light chain-binding domain to the movement, processivity, and directionality of a single-headed processive myosin, we expressed constructs of Caenorhabditis elegans myosin IX (Myo9) containing either the head (Myo9-head) or the head and the light chain-binding domain (Myo9-head-4IQ). Both constructs supported actin filament gliding and moved toward the plus-end of actin filaments. We identified in the head of class IX myosins a calmodulin-binding site at the N terminus of loop 2 that is unique among the myosin superfamily members. Ca(2+)/calmodulin negatively regulated ATPase and motility of the Myo9-head. The Myo9-head demonstrated characteristics of a processive motor in that it supported actin filament gliding and pivoting at low motor densities. Quantum dot-labeled Myo9-head moved along actin filaments with a considerable run length and frequently paused without dissociating even in the presence of obstacles. We conclude that class IX myosins are plus-end-directed motors and that even a single head exhibits characteristics of a processive motor.

Indexed as

ActinsAdenosine TriphosphatasesAnimalsCaenorhabditis elegansCalciumCalmodulinHumansKineticsMass SpectrometryMyosinsPlasmidsProtein BindingProtein Structure, TertiaryQuantum DotsRecombinant ProteinsActinsAdenosine TriphosphatasesCalciumCalmodulinmyosin IXBMyosinsRecombinant Proteins

Identifiers

PMID20538589
PMCPMC2915729

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.