Evidence map›Paper›PMID 21680740›Full record

ArticleThe Journal of biological chemistry2011

Kinesin Kar3Cik1 ATPase pathway for microtubule cross-linking.

Chun Ju Chen, Ivan Rayment, Susan P Gilbert

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Drosophila Ncd reveals an evolutionarily conserved powerstroke mechanism for homodimeric and heterodimeric kinesin-14s.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Article
  8. Kinesin-2 KIF3AB exhibits novel ATPase characteristics.The Journal of biological chemistry · 2014
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Unconventional functions of microtubule motors.Archives of biochemistry and biophysics · 2012
    Review
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.

Chun Ju ChenDepartment of Biology and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180 and.
Ivan RaymentDepartment of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706.
Susan P GilbertDepartment of Biology and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180 and. Electronic address: sgilbert@rpi.edu.

Funding

Mechanistic Analysis of Microtubule Based MotorsR37GM054141 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI GILBERT, SUSAN P. · 2013 to 2022
$4.4M
Mechanistic Analysis Of Microtubule Based MotorsR01GM054141 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GILBERT, SUSAN P. · 1996 to 2012
$3.8M
Structural Studies of Myosin Motor ProteinsR01GM086351 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RAYMENT, IVAN · 2009 to 2010
$586k
Mechanistic Analysis of Microtubule-Based MotorsK02AR047841 · NIAMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GILBERT, SUSAN P. · 2002 to 2006
$509k
NIAMS NIH HHS K02 AR047841NIAMS NIH HHS K02-AR47841NIGMS NIH HHS GM086351NIGMS NIH HHS GM54141NIGMS NIH HHS R01 GM054141NIGMS NIH HHS R01 GM086351NIGMS NIH HHS R37 GM054141
6 · The paper itself

Abstract

Kar3Cik1 is a Saccharomyces cerevisiae kinesin-14 that functions to shorten cytoplasmic microtubules (MTs) during yeast mating yet maintains mitotic spindle stability by cross-linking anti-parallel interpolar MTs. Kar3 contains both an ATP- and a MT-binding site, yet there is no evidence of a nucleotide-binding site in Cik1. Presteady-state and steady-state kinetic experiments were pursued to define the regulation of Kar3Cik1 interactions with the MT lattice expected during interpolar MT cross-linking. The results reveal that association of Kar3Cik1 with the MT occurs at 4.9 μM(-1) s(-1), followed by a 5-s(-1) structural transition that limits ADP release from the Kar3 head. Mant-ATP binding occurred at 2.1 μM(-1) s(-1), and the pulse-chase experiments revealed an ATP-promoted isomerization at 69 s(-1). ATP hydrolysis was observed as a rapid step at 26 s(-1) and was required for the Kar3Cik1 motor to detach from MT. The conformational change at 5 s(-1) that occurred after Kar3Cik1 MT association and prior to ADP release was hypothesized to be the rate-limiting step for steady-state ATP turnover. We propose a model in which Kar3Cik1 interacts with the MT lattice through an alternating cycle of Cik1 MT collision followed by Kar3 MT binding with head-head communication between Kar3 and Cik1 modulated by the Kar3 nucleotide state and intramolecular strain.

Indexed as

Models, BiologicalAdenosine TriphosphatasesBinding SitesMicrotubule-Associated ProteinsMicrotubule ProteinsMicrotubulesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusAdenosine TriphosphatasesCIK1 protein, S cerevisiaeKAR3 protein, S cerevisiaeMicrotubule-Associated ProteinsMicrotubule ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21680740
PMCPMC3190732

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.