Evidence map›Paper›PMID 18775962›Full record

ArticleBiophysical journal2008

Secondary structure and compliance of a predicted flexible domain in kinesin-1 necessary for cooperation of motors.

Alvaro H Crevenna, Sineej Madathil, Daniel N Cohen, Michael Wagenbach, Karim Fahmy, Jonathon Howard

Abstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Intracellular cargo transport by single-headed kinesin motors.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  2. Kinesin rotates unidirectionally and generates torque while walking on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  8. Direct measurements of kinesin torsional properties reveal flexible domains and occasional stalk reversals during stepping.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  9. The reciprocal coordination and mechanics of molecular motors in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

6 authors.

Alvaro H CrevennaMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Sineej Madathil
Daniel N Cohen
Michael Wagenbach
Karim Fahmy
Jonathon Howard

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although the mechanism by which a kinesin-1 molecule moves individually along a microtubule is quite well-understood, the way that many kinesin-1 motor proteins bound to the same cargo move together along a microtubule is not. We identified a 60-amino-acid-long domain, termed Hinge 1, in kinesin-1 from Drosophila melanogaster that is located between the coiled coils of the neck and stalk domains. Its deletion reduces microtubule gliding speed in multiple-motor assays but not single-motor assays. Hinge 1 thus facilitates the cooperation of motors by preventing them from impeding each other. We addressed the structural basis for this phenomenon. Video-microscopy of single microtubule-bound full-length motors reveals the sporadic occurrence of high-compliance states alternating with longer-lived, low-compliance states. The deletion of Hinge 1 abolishes transitions to the high-compliance state. Based on Fourier transform infrared, circular dichroism, and fluorescence spectroscopy of Hinge 1 peptides, we propose that low-compliance states correspond to an unexpected structured organization of the central Hinge 1 region, whereas high-compliance states correspond to the loss of that structure. We hypothesize that strain accumulated during multiple-kinesin motility populates the high-compliance state by unfolding helical secondary structure in the central Hinge 1 domain flanked by unordered regions, thereby preventing the motors from interfering with each other in multiple-motor situations.

Indexed as

MovementAmino Acid SequenceAnimalsDrosophila ProteinsElasticityHumansKinesinsMiceMicrotubulesMolecular Sequence DataPeptidesProtein MultimerizationProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryDrosophila ProteinsKhc protein, DrosophilaKinesinsPeptides

Identifiers

PMID18775962
PMCPMC2586589

What OpenQuestion holds

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Registered trials

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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.