Evidence map›Paper›PMID 24782540›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

CK2 activates kinesin via induction of a conformational change.

Michelle K Mattson-Hoss, Yamato Niitani, Elizabeth A Gordon, Yonggun Jun, Lee Bardwell, Michio Tomishige, Steven P Gross

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Axonal Transport: A Constrained System.Journal of neurology & neuromedicine · 2017
    Article
  3. Review
  4. 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

7 authors.

Michelle K Mattson-HossDevelopmental and Cell Biology, School of Biological Sciences, University of California, Irvine, CA 92697; and.
Yamato NiitaniDepartment of Applied Physics, University of Tokyo, Tokyo 113-8656, Japan.
Elizabeth A GordonDevelopmental and Cell Biology, School of Biological Sciences, University of California, Irvine, CA 92697; and.
Yonggun JunDevelopmental and Cell Biology, School of Biological Sciences, University of California, Irvine, CA 92697; and.
Lee BardwellDevelopmental and Cell Biology, School of Biological Sciences, University of California, Irvine, CA 92697; and.
Michio TomishigeDepartment of Applied Physics, University of Tokyo, Tokyo 113-8656, Japan.
Steven P GrossDevelopmental and Cell Biology, School of Biological Sciences, University of California, Irvine, CA 92697; and sgross@uci.edu.

Funding

Uncover Strategies Used By Biological SystemsP50GM076516 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI LANDER, ARTHUR D · 2007 to 2016
$25.1M
In vivo regulation of bi-directional transportR01GM064624 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI GROSS, STEVEN P · 2002 to 2012
$2.8M
NIGMS NIH HHS P50 GM076516NIGMS NIH HHS P50-GM76516NIGMS NIH HHS R01 GM064624NIGMS NIH HHS R01-GM64624
6 · The paper itself

Abstract

Kinesin is the canonical plus-end microtubule motor and has been the focus of intense study since its discovery in 1985. We previously demonstrated a time-dependent inactivation of kinesin in vitro that was fully reversible by the addition of purified casein kinase 2 (CK2) and showed that this inactivation/reactivation pathway was relevant in cells. Here we show that kinesin inactivation results from a conformational change that causes the neck linker to be positioned closer to the motor domain. Furthermore, we show that treatment of kinesin with CK2 prevents and reverses this repositioning. Finally, we demonstrate that CK2 treatment facilitates ADP dissociation from the motor, resulting in a nucleotide-free state that promotes microtubule binding. Thus, we propose that kinesin inactivation results from neck-linker repositioning and that CK2-mediated reactivation results from CK2's dual ability to reverse this repositioning and to promote ADP release.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsCasein Kinase IIEnzyme ActivationHumansKinesinsMicrotubulesModels, MolecularProtein Structure, TertiarySignal TransductionAdenosine DiphosphateAdenosine TriphosphateCasein Kinase IIKinesinscargo travelmultiple-motor transporttransport regulation

Identifiers

PMID24782540
PMCPMC4024924

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.