Evidence map›Paper›PMID 19278641›Full record

ArticleCurrent biology : CB2009

The processivity of kinesin-2 motors suggests diminished front-head gating.

Gayatri Muthukrishnan, Yangrong Zhang, Shankar Shastry, William O Hancock

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
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  6. Directionally biased sidestepping of Kip3/kinesin-8 is regulated by ATP waiting time and motor-microtubule interaction strength.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Kinesin-2 motors: Kinetics and biophysics.The Journal of biological chemistry · 2018
    Review
  9. Article
  10. Review
  11. Article
  12. Article
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  14. Review
  15. Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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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.

Gayatri MuthukrishnanDepartment of Bioengineering, The Pennsylvania State University, 205 Hallowell Building, University Park, PA 16802, USA.
Yangrong Zhang
Shankar Shastry
William O Hancock
Pennsylvania State University · US

Funding

Molecular mechanism of kinesin motilityR01GM076476 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2006 to 2019
$3.5M
NIGMS NIH HHS GM076476NIGMS NIH HHS R01 GM076476
6 · The paper itself

Abstract

Kinesin-2 motors, which are involved in intraflagellar transport and cargo transport along cytoplasmic microtubules, differ from motors in the canonical kinesin-1 family by having a heterodimeric rather than homodimeric structure and possessing a three amino acid insertion in their neck linker domain. To determine how these structural features alter the chemomechanical coupling in kinesin-2, we used single-molecule bead experiments to measure the processivity and velocity of mouse kinesin-2 heterodimer (KIF3A/B) and the engineered homodimers KIF3A/A and KIF3B/B and compared their behavior to Drosophila kinesin-1 heavy chain (KHC). Single-motor run lengths of kinesin-2 were 4-fold shorter than those of kinesin-1. Extending the kinesin-1 neck linker by three amino acids led to a similar reduction in processivity. Furthermore, kinesin-2 processivity varied inversely with ATP concentration. Stochastic simulations of the kinesin-1 and kinesin-2 hydrolysis cycles suggest that "front-head gating," in which rearward tension prevents ATP binding to the front head when both heads are bound to the microtubule, is diminished in kinesin-2. Because the mechanical tension that underlies front-head gating must be transmitted through the neck linker domains, we propose that the diminished coordination in kinesin-2 is a result of its longer and, hence, more compliant neck linker element.

Indexed as

Protein ConformationAdenosine TriphosphateAmino Acid SequenceAnimalsBiological TransportComputer SimulationDrosophila melanogasterDrosophila ProteinsHumansKinesinsMiceModels, MolecularMolecular Motor ProteinsMolecular Sequence DataProtein BindingSequence AlignmentAdenosine TriphosphateDrosophila Proteinskinesin 2 protein, DrosophilaKinesinsMolecular Motor Proteins

Identifiers

PMID19278641
PMCPMC2730044
OpenAlexW2089611860

What OpenQuestion holds

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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.